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Recombinant Human FGF10 Protein, >95% SDS-PAGE, high purity

  • ActiBioPure™
  • Animal Free
  • Azide Free
  • Bioactive
  • Carrier Free
  • High performance
  • ≥95%(SDS-PAGE)
Features and benefits
  • Expression System: E.coli
  • Accession #: O15520
  • Protein Tag: No tag
  • Bioactivity: Measured in a cell proliferation assay using MCF‑7 human breast cancer cells in the presence of 2 μg/mL of heparin sodium. The ED50 for this effect is typically <21ng/mL.
  • Endotoxin Concentration: <0.1 EU/µg
Item Number
rp145913
Grouped product items
SKUSizeAvailabilityPrice Qty
rp145913-10μg
10μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$139.90
rp145913-25μg
25μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$269.90
rp145913-100μg
100μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$599.90
rp145913-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$2,599.90

Animal Free, >95% SDS-PAGE, Active, E.coli, No tag, Leu40-Ser208

View related series
Accession#:O15520 FGF10 Gene ID:2255

Basic Description

Product NameRecombinant Human FGF10 Protein, >95% SDS-PAGE, high purity
Synonyms FGF10; FGF-10; fibroblast growth factor 10; Keratinocyte growth factor 2; KGF2; KGF-2; produced by fibroblasts of urinary bladder lamina propria; BB213776; fd11d03; FGF 10; FGF10_HUMAN; wu:fd11d03; zgc:109774
GradeActiBioPure™, Animal Free, Azide Free, Bioactive, Carrier Free, High performance
Product Description

Purity

≥ 95% SDS-PAGE.


Additional sequence information

Mature chain.


Function

Could be a growth factor active in the process of wound healing. Acts as a mitogen in the lung. May act in a manner similar to FGF-7.

Specifications & PurityActiBioPure™, Bioactive, Animal Free, Carrier Free, Azide Free, High performance, ≥95%(SDS-PAGE)
Purity>95% SDS-PAGE
BioactivityMeasured in a cell proliferation assay using MCF‑7 human breast cancer cells in the presence of 2 μg/mL of heparin sodium. The ED50 for this effect is typically <21ng/mL.
Endotoxin Concentration<0.1 EU/µg
Expression SystemE.coli
SpeciesHuman
Amino Acids40-208 aa
SequenceLGQDMVSPEATNSSSSSFSSPSSAGRHVRSYNHLQGDVRWRKLFSFTKYFLKIEKNGKVSGTKKENCPYSILEITSVEIGVVAVKAINSNYYLAMNKKGKLYGSKEFNNDCKLKERIEENGYNTYASFNWQHNGRQMYVALNGKGAPRRGQKTRRKNTSAHFLPMVVHS
Protein TagNo tag
Protein LengthFull length protein
Accession #O15520
SourceRecombinant
Predicted molecular weight19.3 kDa
SDS-PAGE19.8 kDa, under reducing conditions; 19.8 kDa, under non-reducing conditions.

Images

Recombinant Human FGF10 Protein (rp145913)-Protein Bioactivity
Measured in a cell proliferation assay using MCF‑7 human breast cancer cells in the presence of 2 μg/mL of heparin sodium. The ED₅₀ for this effect is typically <21ng/mL.

Recombinant Human FGF10 Protein (rp145913)-SDS-PAGE
3μg/lane of Recombinant Human FGF10 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a single band at 19.8 kDa.

Product Specifications

FormLyophilized
ReconstitutionCentrifuge first and redissolve with deionized water to proposal concentration.
Storage TempStore at -20°C
Shipped InIce chest + Ice pads
Stability And StorageShipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Certificates

Certificate of Analysis(COA)

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2 results found

Lot NumberCertificate TypeDateItem
ZJ23F1001346Certificate of AnalysisOct 19, 2023 rp145913
ZJ23F1001347Certificate of AnalysisOct 19, 2023 rp145913

Related Documents

References

1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P et al..  (2004)  The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)..  Genome Res,  14  (10B): (2121-7).  [PMID:15489334]
2. Yeh BK, Igarashi M, Eliseenkova AV, Plotnikov AN, Sher I, Ron D, Aaronson SA, Mohammadi M.  (2003)  Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors..  Proc Natl Acad Sci USA,  100  (5): (2266-71).  [PMID:12591959]
3. Emoto, H H and 10 more authors..  (1997)  Structure and expression of human fibroblast growth factor-10..  The Journal of biological chemistry,    (12):   [PMID:9287324]
4. Entesarian, Miriam M and 12 more authors..  (2005)  Mutations in the gene encoding fibroblast growth factor 10 are associated with aplasia of lacrimal and salivary glands..  Nature genetics,      [PMID:15654336]
5. Beer, Hans-Dietmar HD and 6 more authors..  (2005)  The fibroblast growth factor binding protein is a novel interaction partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity: implications for epithelial repair..  Oncogene,    (11):   [PMID:15806171]
6. Rohmann, Edyta E and 21 more authors..  (2006)  Mutations in different components of FGF signaling in LADD syndrome..  Nature genetics,      [PMID:16501574]
7. Zhang, Xiuqin X and 5 more authors..  (2006)  Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family..  The Journal of biological chemistry,    (9):   [PMID:16597617]
8. Milunsky, J M JM, Zhao, G G, Maher, T A TA, Colby, R R and Everman, D B DB..  (2006)  LADD syndrome is caused by FGF10 mutations..  Clinical genetics,      [PMID:16630169]

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