Description:

Size: 100ul

Catalog no.: bs-0463R-A594

Price: 380 EUR

Product details

Modification Site

None

Target Antigen

MMP-1

Gene ID Number

300339

Subcellular location

Secreted

French translation

anticorps

Tested applications

IF(IHC-P)

Clonality

Polyclonal

Crossreactivity

Mouse, Rat

Modification

Unmodified

Excitation emission

590nm/617nm

Immunogen range

430-464/464

Concentration

1ug per 1ul

Conjugated with

ALEXA FLUOR® 594

Conjugated

Alexa conjugate 1

Recommended dilutions

IF(IHC-P)(1:50-200)

Clone

Polyclonal antibody

Purification

Purified by Protein A.

Category

Conjugated Primary Antibodies

Conjugation

Alexa Fluor,ALEXA FLUOR® 594

Host Organism

Rabbit (Oryctolagus cuniculus)

Also known as

Anti-MMP-1 PAb ALEXA FLUOR 594

Specificity

This is a highly specific antibody against MMP-1.

Long name

MMP-1 Polyclonal Antibody, ALEXA FLUOR 594 Conjugated

Source

KLH conjugated synthetic peptide derived from rat MMP1

Cross-reactive species details

Due to limited amount of testing and knowledge, not every possible cross-reactivity is known.

Storage conditions

Store this antibody in aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Keep refrigerated at 2 to 8 degrees Celcius for up to one year.

Properties

For facs or microscopy Alexa 1 conjugate.If you buy Antibodies supplied by Bioss Primary Conjugated Antibodies. ALEXA FLUOR they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.

Synonyms

CLGN; CLG; 27 kDa interstitial collagenase; collagenase, fibroblast; Fibroblast collagenase; Interstitial collagenase; Matrix metallopeptidase 1 interstitial collagenase; Matrix metalloproteinase-1; Matrix metalloprotease 1; Matrix Metalloproteinase 1; MMP-1; MMP1; MMP1_HUMAN; OTTHUMP00000045866; MMP 1.

Background of the antigen

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.