antibody

Gelatin, Skin

MBS625052

0.1 mL

720 USD

polyclonal

rabbit

nonconjugated

rat, cow

ELISA, other

Antibody

Gelatin, Skin

[Gelatin, Skin]

[Anti -Gelatin, Skin]

[gelatinase B; Matrix metalloproteinase-9; matrix metalloproteinase-9; GELB; MMP-9; gelatinase B; 92 kDa gelatinase; 92 kDa type IV collagenase; 92-kDa type IV collagenase; matrix metalloproteinase 9 (gelatinase B 92-kDa type IV collagenase); matrix metalloproteinase 9 (gelatinase B, 92-kDa type IV collagenase); matrix metallopeptidase 9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B]

[Mmp9; Mmp9; MMP-9; GELB]

MMP9_RAT

Polyclonal

IgG

Rabbit

Bovine

Recognizes bovine skin gelatin.

Serum

Supplied as a lyophilized powder from PBS, 0.05% sodium azide. Reconstitute with 100ul sterile PBS.

Lyophilized powder may be stored at -20°C. Stable for 12 months after receipt at -20°C. Reconstitute with sterile PBS. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Suitable for use in ELISA. Other applications not tested.

Dilution: ELISA: 1:1000-1:10,000; Coat gelatin antigen at 5-10ug/ml. Optimal dilutions to be determined by the researcher.

Immunogen: Gelatin, bovine skin Type B

Antibodies; Abs to Collagen

Gelatin is a heterogeneous mixture of water-soluble proteins of high average molecular weights, present in collagen. The proteins are extracted by boiling skin, tendons, ligaments, bones, etc. in water. Type A gelatin is derived from acid-cured tissue and Type B gelatin is derived from lime-cured tissue. The charge on a gelatin molecule and its isoelectric point are primarily due to the carboxyl amino and guanidino groups on the side chains. Type A gelatin has 78-80 millimoles of free carboxyl groups per 100g of protein and a pI of 7.0-9.0; type B has 100-115 millimoles of free carboxyl groups per 100g of protein and a pI of 4.7-5.2. The pH of a 1.5% solution at 25°C is 3.8-5.5 for Type A and 5.0-7.5 for Type B. Applications using gelatin include coating cell culture plates to improve cell attachment for a variety of cell types, addition to PCR to help stabilize Taq DNA polymerase, and use as a blocking reagent in Western Blot, ELISA, and Immunohistochemistry. In bacteriology, gelatin can be used as a component of culture media for species differentiation. Additionally, as a biocompatible polymer, gelatin has been used as a delivery vehicle for the release of bioactive molecules and in the generation of scaffolds for tissue engineering applications. Gelatin proteins are also used as additives in purified, recombinant proteins and antibodies. Animals or humans exposed to gelatins may invoke antibody response. Often the gelatin must be removed prior to such applications. Antibodies to gelatins were produced to detect the presence of gelatins in biolgocial samples and or to verify their removal during bioprocess development.

1173506

AAA90911.1

P50282

Bladder Cancer Pathway (83503); Bladder Cancer Pathway (527); Endochondral Ossification Pathway (219771); Estrogen Signaling Pathway (799190); Estrogen Signaling Pathway (799197); Hepatitis B Pathway (694795); IL-3 Signaling Pathway (198504); Leukocyte Transendothelial Migration Pathway (83475); Leukocyte Transendothelial Migration Pathway (494); Matrix Metalloproteinases Pathway (198492)

metalloproteinase involved in extracellular matrix remodeling and bone resorption [RGD, Feb 2006]

Function: Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments . By similarity. Catalytic activity: Cleavage of gelatin types I and V and collagen types IV and V. Cofactor: Binds 2 zinc ions per subunit . By similarity.Binds 3 calcium ions per subunit . By similarity. Subunit structure: Exists as monomer or homodimer; disulfide-linked . By similarity. Exists also as heterodimer with a 25 kDa protein . By similarity. Interacts with ECM1 . By similarity. Subcellular location: Secreted extracellular space extracellular matrix . Probable. Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. Post-translational modification: N- and O-glycosylated . By similarity. Sequence similarities: Belongs to the peptidase M10A family.Contains 3 fibronectin type-II domains.Contains 4 hemopexin repeats.

0.1 mL

720 USD