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Supplier: Biotium

Description: This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with all subclasses of Alpha heavy chain. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Supplier: Biotium

Description: This MAb recognizes a 22 kDa protein, identified as Transgelin, also designated SM22-alpha. It may cross-react with SM22-beta. Transgelin is expressed abundantly in smooth muscle cells. The human transgelin gene encodes a 201 amino acid protein that contains nuclear factor-binding motifs known to regulate transcription in smooth muscle. During embryogenesis, transgelin is expressed in smooth, cardiac and skeletal muscle, but is restricted during late fetal development and adulthood to all vascular and visceral smooth muscle cells and low levels of expression in heart. Transgelin is down regulated in several transformed cell lines, indicating that a reduction of transgelin expression may be an early indicator of the onset of transformation. Transgelin also binds Actin, causing Actin fibers to gel within minutes of binding. Binding of transgelin to Actin occurs at a ratio of 1:6 Actin monomers.

Supplier: Biotium

Description: Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for anti-thyroglobulin even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently anti-thyroglobulin negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Anti-thyroglobulin, combined with anti-calcitonin, can identify medullary carcinomas of the thyroid. Furthermore, anti-thyroglobulin, combined with anti-TTF1, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.

Supplier: Biotium

Description: Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for anti-thyroglobulin even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently anti-thyroglobulin negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Anti-thyroglobulin, combined with anti-calcitonin, can identify medullary carcinomas of the thyroid. Furthermore, anti-thyroglobulin, combined with anti-TTF1, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.

Catalog Number: (BOSSBS-7548R-A555)

Supplier: Bioss

Description: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.

UOM: 1 * 100 µl

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Catalog Number: (ENZOALX801051L001)

Supplier: ENZO LIFE SCIENCES

Description: Gross cystic disease is a common premenopausal disorder in which gross cysts are the predominant pathologic lesion. It is characterized by production of a fluid secretion which accumulates in the breast cysts. Gross cystic disease fluid is a pathologic secretion from breast composed of several glycoproteins, including a unique 15kDa monomer protein, GCDFP-15. The cells within the body that produce GCDFP-15 appear to be restricted primarily to those with apocrine function. Studies have found GCDFP-15 to be a highly specific and sensitive marker for breast cancer.
GCDFP-15 is expressed by apocrine sweat glands, eccrine glands (variable), minor salivary glands, bronchial glands, metaplasmic epithelium of the breast, benign sweat gland tumors of the skin and the serous cells of the submandibular gland. Breast carcinomas (primary and metastatic lesions) with apocrine features express GCDFP-15. GCDFP-15 is positive in extramammary Paget's Disease. Other tumors tested are negative.

UOM: 1 * 1 mL

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Catalog Number: (BOSSBS-13189R-A350)

Supplier: Bioss

Description: Amines, including those present on proteins, spontaneously react with glucose to make fructosamines in a reaction termed glycation. Fructosamine 3-kinase (FN3K), a 309-amino acid enzyme initially identified in erythrocytes, catalyzes the ATP-dependent phosphorylation of the third carbon on both D- and L-fructosamines, leading to their destabilization and eventually, their removal from the protein. FN3K is a monomer that is ubiquitously expressed in mammalian tissue and phosphorylates both low molecular mass and protein-bound fructosamines which are formed as a result of glycation of glucose with primary amines. FN3K protects proteins from the harmful effects of nonenzymatic glycation, and may also be involved in peptide repair and cell metabolism. FN3KRP (fructosamine-3-kinase-related protein) is a 309 amino acid protein that is expressed in erythrocytes, bone marrow, spleen, brain and kidney and belongs to the fructosamine kinase family. FN3KRP functions to phosphorylate psicoamines and ribulosamines on the third carbon of their sugar moiety, thereby leading to the deglycation of the target amines.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13189R-A555)

Supplier: Bioss

Description: Amines, including those present on proteins, spontaneously react with glucose to make fructosamines in a reaction termed glycation. Fructosamine 3-kinase (FN3K), a 309-amino acid enzyme initially identified in erythrocytes, catalyzes the ATP-dependent phosphorylation of the third carbon on both D- and L-fructosamines, leading to their destabilization and eventually, their removal from the protein. FN3K is a monomer that is ubiquitously expressed in mammalian tissue and phosphorylates both low molecular mass and protein-bound fructosamines which are formed as a result of glycation of glucose with primary amines. FN3K protects proteins from the harmful effects of nonenzymatic glycation, and may also be involved in peptide repair and cell metabolism. FN3KRP (fructosamine-3-kinase-related protein) is a 309 amino acid protein that is expressed in erythrocytes, bone marrow, spleen, brain and kidney and belongs to the fructosamine kinase family. FN3KRP functions to phosphorylate psicoamines and ribulosamines on the third carbon of their sugar moiety, thereby leading to the deglycation of the target amines.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13189R-A647)

Supplier: Bioss

Description: Amines, including those present on proteins, spontaneously react with glucose to make fructosamines in a reaction termed glycation. Fructosamine 3-kinase (FN3K), a 309-amino acid enzyme initially identified in erythrocytes, catalyzes the ATP-dependent phosphorylation of the third carbon on both D- and L-fructosamines, leading to their destabilization and eventually, their removal from the protein. FN3K is a monomer that is ubiquitously expressed in mammalian tissue and phosphorylates both low molecular mass and protein-bound fructosamines which are formed as a result of glycation of glucose with primary amines. FN3K protects proteins from the harmful effects of nonenzymatic glycation, and may also be involved in peptide repair and cell metabolism. FN3KRP (fructosamine-3-kinase-related protein) is a 309 amino acid protein that is expressed in erythrocytes, bone marrow, spleen, brain and kidney and belongs to the fructosamine kinase family. FN3KRP functions to phosphorylate psicoamines and ribulosamines on the third carbon of their sugar moiety, thereby leading to the deglycation of the target amines.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6216R-CY3)

Supplier: Bioss

Description: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity (By similarity)

UOM: 1 * 100 µl

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Supplier: ENZO LIFE SCIENCES

Description: Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.

Catalog Number: (BNUM0148-50)

Supplier: Biotium

Description: This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with both IgA1 and IgA2 subclasses of Alpha heavy chain. It reacts with the third constant domain (CH3) of the alpha chain of IgA molecules. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

UOM: 1 * 50 µl

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Catalog Number: (ORIGTA183039)

Supplier: OriGene

Description: Anti-DsRed-Monomer IgG1 Monoclonal Antibody (Magnetic beads) [clone: OTI4C7 (formerly 4C7)]

UOM: 1 * 1 mL

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Catalog Number: (BOSSBS-10493R-CY5)

Supplier: Bioss

Description: Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi. Multiple alternatively spliced transcript variants that encode the same proteins have been identified.[provided by RefSeq, Sep 2008].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11871R-FITC)

Supplier: Bioss

Description: LIMK 1 and 2 likely regulate aspects of the cytoskeleton, through control of the organization of actin filaments. They can phosphorylate an actin-binding protein, cofilin which binds to actin monomers and polymers and promotes the disassembly of actin filament.The phosphorylation of cofilin via LIMK inactivates this potential. LIMK1 is highly active in the brain and spinal chord, where it is believed to be involved in the development of nerve cells whilst LIMK2 is ubiquitously expressed in many adult tissues. LIMK1 may play an important role in areas of the brain that are responsible for processing visual-spatial information (visuospatial constructive cognition). These parts of the brain are important for visualizing an object as a set of parts and performing tasks such as writing, drawing, constructing models, and assembling puzzles. LIMK1 is specifically stimulated by Rac, one of the Rho family proteins, while LIMK2 activity is activated under the control of other Rho family members, Rho and Cdc42, suggesting that two distinct pathways exist in the Rho family driven actin cytoskeleton dynamics.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11871R-A488)

Supplier: Bioss

Description: LIMK 1 and 2 likely regulate aspects of the cytoskeleton, through control of the organization of actin filaments. They can phosphorylate an actin-binding protein, cofilin which binds to actin monomers and polymers and promotes the disassembly of actin filament.The phosphorylation of cofilin via LIMK inactivates this potential. LIMK1 is highly active in the brain and spinal chord, where it is believed to be involved in the development of nerve cells whilst LIMK2 is ubiquitously expressed in many adult tissues. LIMK1 may play an important role in areas of the brain that are responsible for processing visual-spatial information (visuospatial constructive cognition). These parts of the brain are important for visualizing an object as a set of parts and performing tasks such as writing, drawing, constructing models, and assembling puzzles. LIMK1 is specifically stimulated by Rac, one of the Rho family proteins, while LIMK2 activity is activated under the control of other Rho family members, Rho and Cdc42, suggesting that two distinct pathways exist in the Rho family driven actin cytoskeleton dynamics.

UOM: 1 * 100 µl

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