Přejít k obsahu
Merck
Všechny fotografie(2)

Key Documents

MAB1973

Sigma-Aldrich

Anti-Integrin α1 Antibody, clone FB12

clone FB12, Chemicon®, from mouse

Synonyma:

CD49a

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


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

FB12, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG1

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... ITGA1(3672)

Specificity

Reacts with the I domain (Val151 - Ala364) of human alpha-1 integrin (CD49a)1. Precipitates proteins of Mr 180 kDa, pI 5.9-6.0 (alpha chain) and Mr 115 kDa, pI 4.5-5.0 (beta chain) from human lymphocyte lysates (Zocchi et al., 1991).

Application

Immunohistochemistry: 2 μg/mL, with paraformaldehyde fixation.
Immunohistochemistry: Frozen sections (7 µm) of placental tissue fixed with acetone for 1 hr. Antibody used at 1:10 dilution (Sato et al., 2003).
Immunocytochemistry: iolated EVT cells firxed with 0.5% PFA @ 4°C for 15 minutes followed by acetone at -20°C for 2 minutes. Antibody was used at 1:10 dilution (Sato et al., 2003).
Immunoblotting: 2 μg/mL

Immunoprecipitation: 1 μg/mL

FACS analysis: 2μg/mL (Sato et al., 2005).

ELISA: 0.5 μg/mL

Inhibition of activated human lymphocyte binding to laminin, collagen IV and fibronectin (Fabbri et al., 1996): 1-5 μg/mL

Optimal working dilutions must be determined by end user.
This Anti-Integrin α1 Antibody, clone FB12 is validated for use in ELISA, FC, IC, IH, IP, FUNC, WB for the detection of Integrin α1.

Target description

130 kDa

Physical form

Format: Purified
Purified immunoglobulin in 0.02M PB, pH 7.6, 0.25M NaCl containing 0.1% sodium azide.

Analysis Note

Control
Microvascular endothelium

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

Ještě jste nenalezli správný produkt?  

Vyzkoušejte náš produkt Nástroj pro výběr produktů.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Osvědčení o analýze (COA)

Vyhledejte osvědčení Osvědčení o analýze (COA) zadáním čísla šarže/dávky těchto produktů. Čísla šarže a dávky lze nalézt na štítku produktu za slovy „Lot“ nebo „Batch“.

Již tento produkt vlastníte?

Dokumenty související s produkty, které jste v minulosti zakoupili, byly za účelem usnadnění shromážděny ve vaší Knihovně dokumentů.

Navštívit knihovnu dokumentů

Leo K Iwai et al.
The Biochemical journal, 454(3), 501-513 (2013-07-05)
Collagen is an important extracellular matrix component that directs many fundamental cellular processes including differentiation, proliferation and motility. The signalling networks driving these processes are propagated by collagen receptors such as the β1 integrins and the DDRs (discoidin domain receptors).
M A Sanders et al.
The Journal of biological chemistry, 275(48), 38040-38047 (2000-09-15)
Integrin-initiated extracellular signal-regulated kinase (ERK) activation by matrix adhesion may require focal adhesion kinase (FAK) or be FAK-independent via caveolin and Shc. This remains controversial for fibroblast and endothelial cell adhesion to fibronectin and is less understood for other matrix
B K Pilcher et al.
The Journal of cell biology, 137(6), 1445-1457 (1997-06-16)
We have shown in a variety of human wounds that collagenase-1 (MMP-1), a matrix metalloproteinase that cleaves fibrillar type I collagen, is invariably expressed by basal keratinocytes migrating across the dermal matrix. Furthermore, we have demonstrated that MMP-1 expression is
Katarzyna Biadasiewicz et al.
Endocrinology, 152(4), 1458-1469 (2011-02-10)
The basic helix-span-helix transcription factor activating protein (AP)-2α is critically involved in cell-specific hormone expression of syncytializing human trophoblasts. Its role in invasive trophoblast differentiation, however, remains largely elusive. Using RT-PCR, Western blotting, and immunofluorescence of first-trimester placentae, we here
Huifang Xu et al.
PloS one, 7(12), e52209-e52209 (2013-01-04)
The discoidin domain receptors, DDR1 and DDR2, are receptor tyrosine kinases that bind to and are activated by collagens. Similar to collagen-binding β1 integrins, the DDRs bind to specific motifs within the collagen triple helix. However, these two types of

Náš tým vědeckých pracovníků má zkušenosti ve všech oblastech výzkumu, včetně přírodních věd, materiálových věd, chemické syntézy, chromatografie, analytiky a mnoha dalších..

Obraťte se na technický servis.