Reactive species
Human;Mouse;Rat
Antibody type
Polyclonal Antibody
Protein name
Latent-transforming growth factor beta-binding protein 1 (LTBP-1) (Transforming growth factor beta-1-binding protein 1) (TGF-beta1-BP-1)
Immunogen
Synthesized peptide derived from part region of human protein
Specificity
LTBP1 Polyclonal Antibody detects endogenous levels of protein.
Constitute
Liquid in PBS containing 50% glycerol, and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
WB 1:500-2000 ELISA 1:5000-20000
Purification process
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Background
latent transforming growth factor beta binding protein 1(LTBP1) Homo sapiens The protein encoded by this gene belongs to the family of latent TGF-beta binding proteins (LTBPs). The secretion and activation of TGF-betas is regulated by their association with latency-associated proteins and with latent TGF-beta binding proteins. The product of this gene targets latent complexes of transforming growth factor beta to the extracellular matrix, where the latent cytokine is subsequently activated by several different mechanisms. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008],
Function
domain:Associates covalently with small latent TGF-beta complex via domain TB 3.,function:May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM).,PTM:Contains hydroxylated asparagine residues.,PTM:The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.,PTM:The N-terminus is blocked (isoform Short).,similarity:Belongs to the LTBP family.,similarity:Contains 18 EGF-like domains.,similarity:Contains 4 TB (TGF-beta binding) domains.,subunit:The large latent complex of TGFB1 from platelets is composed of the TGFB1 molecule non-covalently associated with a disulfide-bonded complex of a dimer of the N-terminal propeptide of the TGFB1
