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MAB1992

Sigma-Aldrich

Anti-Integrin α3β1 Antibody, clone M-KID2

clone M-KID2, Chemicon®, from mouse

Synonym(s):

VLA-3

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

M-KID2, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
radioimmunoassay: suitable

isotype

IgG1

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... ITGA3(3675)

General description

Integrins are a family of dimeric proteins that mediate cell-cell and extracellular matrix adhesion. Each VLA subtype (VLA-1, VLA-2, VL-3, VLA-4, VLA-5) is composed of a distinct alpha subunit noncovalently associated with a common beta subunit, as an alpha-beta dimer. Integrin VLA-3 (very late antigen, alpha-3/beta-1) is a cell surface receptor that binds to fibronectin, laminin, collagen type I and VI. VLA-3 is typically restricted in normal tissue but is widely expressed in many cultured tumor cells and correlates with the degree of invasiveness of malignant melanoma cells.

Specificity

Recognizes an epitope related to the VLA-3 complex (alpha-3/beta-1 integrin). Specificity was determined by immunoprecipitation from a detergent extract of 35S-methionine labeled KJ29 cells.

Immunogen

Human renal carcinoma cell line (KJ29).

Application



Immunohistochemistry (works on Acetone-fixed paraffin-embedded tissues)

ELISA/RIA

Immunoprecipitation. When immunoprecipitated samples are run on SDS-PAGE under a) non-reducing conditions, two bands will be detected with an apparent molecular weight of 110 and 150kDa; and b) reducing (2% B-ME) conditions, a single molecular species of 130kDa is detected. Under reducing conditions both alpha3 and beta1 subunits run with the same apparent molecular weight.

Optimal working dilutions must be determined by end user.
Anti-Integrin α3β1 Antibody, clone M-KID2 detects level of Integrin α3β1 & has been published & validated for use in ELISA, IP, RIA, IC, IH(P).

Physical form

Format: Purified
Immunoglobulin purified by Protein A. Purified immunoglobulin in PBS and 0.05% sodium azide as preservative.

Storage and Stability

Maintain at 2°-8°C in undiluted aliquots for up to 12 months from date of receipt.

Analysis Note

Control
Cell line: KJ29 renal carcinoma adherent cells.
Tissue: Kidney; antibody reacts with basal layer podocytes and basement membrane of distal tubules.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Generation and characterization of the murine monoclonal antibody M-KID 2 to VLA-3 integrin.
Bartolazzi, A, et al.
Hybridoma, 10, 707-720 (1991)
Involvement of specific integrins in apoptosis induced by vascular apoptosis-inducing protein 1.
Satohiko Araki, Shinako Masuda, Hiroki Maeda, Miao Jun Ying, Hiroshi Hayashi
Toxicon null
Mehrnoosh Saghizadeh et al.
Brain research bulletin, 81(2-3), 262-272 (2009-10-16)
Our previous data suggested the involvement of matrix metalloproteinase-10 (MMP-10) and cathepsin F (CTSF) in the basement membrane and integrin changes occurring in diabetic corneas. These markers were now examined in normal human organ-cultured corneas upon recombinant adenovirus (rAV)-driven transduction
Plasminogen activator inhibitors regulate cell adhesion through a uPAR-dependent mechanism.
Ralf-Peter Czekay,David J Loskutoff
Journal of Cellular Physiology null
Mehrnoosh Saghizadeh et al.
Experimental eye research, 129, 66-73 (2014-12-03)
Overexpression of c-met and suppression of matrix metalloproteinase-10 (MMP-10) and cathepsin F genes was previously shown to normalize wound healing, epithelial and stem cell marker patterns in organ-cultured human diabetic corneas. We now examined if gene therapy of limbal cells

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