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CP18 Anti-Collagen Type II (Ab-1) Mouse mAb (II-4C11)

CP18
Purchase on Sigma-Aldrich

Áttekintés

Replacement Information

Kulcsspecifikációk táblázata

Species ReactivityHostAntibody Type
B, H, Rb, RMMonoclonal Antibody

Products

KatalógusszámCsomagolás Menny./csomag
CP18-100UG Plastic Bag(s) 100 μg
Description
OverviewRecognizes the ~130 kDa type II collagen protein. May react with other collagens. When used at high concentrations higher bands corresponding to aggregates may also be detected.
Catalogue NumberCP18
Brand Family Calbiochem®
References
ReferencesKumagai, J. et al. 1994 J. Anat. 185, 278.
Kivrikko, K,I. 1993 Ann. Med. 25, 113.
Sandell, L.J., et al. 1991 J. Cell. Biol. 114, 1307.
Ryan, M.C., and Sandell, L.J. 1990 J. Biol. Chem. 265, 10334.
Mayne, R., and Burgeson, R.E. 1987 Structure and Function of Collagen Types,Academic Press, Orlando, FL
Product Information
DeclarationManufactured by Daiichi Fine Chemical Co., Ltd. Not available for sale in Japan.
FormLiquid
FormulationIn 100 mM sodium phosphate buffer, 0.1% BSA, pH 7.0.
Preservative≤0.1% sodium azide
Quality LevelMQ100
Applications
Application ReferencesImmunoblotting Kumagai, J. et al. 1994 J. Anat. 185, 278. Paraffin Sections Kumagai, J. et al. 1994 J. Anat. 185, 278.
Key Applications Frozen Sections
Immunoblotting (Western Blotting)
Paraffin Sections
Application NotesFrozen Sections (1-10 µg/ml)
Immunoblotting (1-5 µg/ml, see application references)
Paraffin Sections (1-10 µg/ml, see application references)
Application CommentsMay react with other collagens. When used at high concentrations higher bands corresponding to aggregates may also be detected. This antibody may also react with other classes of collagen at a concentration higher than 1 µg/ml. In immunoblotting, a major band of ~130 kDa is obtained. Antibody should be titrated for optimal results in individual systems.
Biological Information
Immunogenpurified collagen type II
ImmunogenHuman
CloneII-4C11
HostMouse
IsotypeIgG₁
Species Reactivity
  • Bovine
  • Human
  • Rabbit
  • Rat
Antibody TypeMonoclonal Antibody
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Blue Ice Only
Toxicity Standard Handling
Storage -20°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Katalógusszám GTIN
CP18-100UG 04055977220957

Documentation

Anti-Collagen Type II (Ab-1) Mouse mAb (II-4C11) MSDS

Title

Safety Data Sheet (SDS) 

Anti-Collagen Type II (Ab-1) Mouse mAb (II-4C11) Certificates of Analysis

TitleLot Number
CP18

References

Hivatkozások áttekintése
Kumagai, J. et al. 1994 J. Anat. 185, 278.
Kivrikko, K,I. 1993 Ann. Med. 25, 113.
Sandell, L.J., et al. 1991 J. Cell. Biol. 114, 1307.
Ryan, M.C., and Sandell, L.J. 1990 J. Biol. Chem. 265, 10334.
Mayne, R., and Burgeson, R.E. 1987 Structure and Function of Collagen Types,Academic Press, Orlando, FL
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision10-July-2007 JSW
ApplicationFrozen Sections (1-10 µg/ml)
Immunoblotting (1-5 µg/ml, see application references)
Paraffin Sections (1-10 µg/ml, see application references)
DescriptionPurified mouse monoclonal antibody generated by immunizing BALB/c mice with the specified immunogen and fusing splenocytes with P3-X-63-Ag8-LUI mouse myeloma cells. Recognizes the ~130 kDa type II collagen protein.
BackgroundCollagens are the major fibrous structural elements of cartilage, tendon, skin, bone, lung and blood vessels. Their function is to hold cells together and thereby form discrete tissues. Collagens form insoluble fibers that have a high intrinsic tensile strength. Structurally, the collagens are composed of three polypeptide chains, αchains, which exist as three distinct subclasses each of which in turn is made up of numerous subtypes. Type II collagen is a major component of cartilage. It is translated as a pro-form which is then processed to yield the mature protein. Collagen II can also be expressed in two different forms, IIA and IIB, as a result of alternate splicing involving the inclusion of exon. The protein is synthesized primarily by chondrocytes and by certain cells in the eye, and exists as a trimer of α1(II) chains. Mutations in collagen II have been documented in chondrodysplasias and ostoarthrosis.
HostMouse
Immunogen speciesHuman
Immunogenpurified collagen type II
CloneII-4C11
IsotypeIgG₁
Speciesbovine, human, rabbit, rat
FormLiquid
FormulationIn 100 mM sodium phosphate buffer, 0.1% BSA, pH 7.0.
Concentration Label Please refer to vial label for lot-specific concentration
Preservative≤0.1% sodium azide
CommentsMay react with other collagens. When used at high concentrations higher bands corresponding to aggregates may also be detected. This antibody may also react with other classes of collagen at a concentration higher than 1 µg/ml. In immunoblotting, a major band of ~130 kDa is obtained. Antibody should be titrated for optimal results in individual systems.
Storage Avoid freeze/thaw
-20°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
Toxicity Standard Handling
ReferencesKumagai, J. et al. 1994 J. Anat. 185, 278.
Kivrikko, K,I. 1993 Ann. Med. 25, 113.
Sandell, L.J., et al. 1991 J. Cell. Biol. 114, 1307.
Ryan, M.C., and Sandell, L.J. 1990 J. Biol. Chem. 265, 10334.
Mayne, R., and Burgeson, R.E. 1987 Structure and Function of Collagen Types,Academic Press, Orlando, FL
Application referencesImmunoblotting Kumagai, J. et al. 1994 J. Anat. 185, 278. Paraffin Sections Kumagai, J. et al. 1994 J. Anat. 185, 278.