Search: 1000 results found for "pdgf"

Description:

Protocadherin Gamma Subfamily C 4 Human Recombinant

Protocadherin Gamma Subfamily C 4, PCDH-GAMMA-C4.

Product # :

PRO-1844

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Description

PCDHGC4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 684 amino acids (30-692) and having a molecular mass of 74.3 kDa. PCDHGC4 is fused to a 21 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The PCDHGC4 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
PCDHGL4 belongs to one of three related clusters tandemly linked on chromosome five - the protocadherin gamma gene cluster. These gene clusters have an immunoglobulin-like organization, which indicates that a novel mechanism takes part in their regulation and expression. These neural cadherin-like cell adhesion proteins have a vital role in the establishment and function of specific cell-cell connections in the brain.
Synonyms
Protocadherin Gamma Subfamily C 4, PCDH-GAMMA-C4.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQIRYPVPEE SQEGTFVGNV AQDFLLDTDS LSARRLQVAG EVNQRHFRVD LDSGALLIKN PIDREALCGL SASCIVPLEF VTEGPLEMYR AEVEIVDVND HAPRFPRQQL DLEIGEAAPP GQRFPLEKAQ DADVGSNSIS SYRLSSNEHF ALDVKKRSDG SLVPELLLEK PLDREKQSDY RLVLTAVDGG NPPRSGTAEL RVSVLDVNDN APAFQQSSYR ISVLESAPAG MVLIQLNASD PDLGPSGNVT FYFSGHTPDR VRNLFSLHPT TGKLTLLGPL DFESENYYEF DVRARDGGSP AMEQHCSLRV DLLDVNDNAP YITVTSELGT LPESAEPGTV VALISVQDPD SGSNGDVSLR IPDHLPFALK SAFRNQFSLV TAGPLDREAK SSYDIMVTAS DAGNPPLSTH RTIFLNISDV NDNPPSFFQR SHEVFVPENN RPGDLLCSLA ASDPDSGLNA LISYSLLEPR NRDVSASSFI SLNPQTGAVH ATRSFDYEQT QTLQFEVQAR DRGNPPLSST VTVRLFVLDL NDNAPAVLRP RARPGSLCPQ ALPPSVGAGH LITKVTAVDL DSGYNAWVSY QLLEAPDPSL FAVSRYAGEV RTAVPIPADL PPQKLVIVVK DSGSPPLSTS VTLLVSLEED THPVVPDLRE SSAPREGESR LTLY

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

p53 and DNA-Damage Regulated 1 Human Recombinant

p53 and DNA damage-regulated protein 1, PDRG1, C20orf126, PDRG.

Product # :

PRO-007

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Description

PDRG1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 153 amino acids (1-133 a.a.) and having a molecular mass of 17.6kDa. The PDRG1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PDRG1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
PDRG1 is a 133 amino acid protein that localizes to the cytoplasm and belongs to the prefoldin subunit beta family. PDRG1 is expressed primarily in normal testicular tissue, it is functionally induced by ultraviolet light and is thought to have a role in chaperone-mediated protein folding, possibly having a role in cellular degradation. PDRG1 is linked to Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome.
Synonyms
p53 and DNA damage-regulated protein 1, PDRG1, C20orf126, PDRG.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLSPEAERVL RYLVEVEELA EEVLADKRQI VDLDTKRNQN REGLRALQKD LSLSEDVMVC FGNMFIKMPH PETKEMIEKD QDHLDKEIEK LRKQLKVKVN RLFEAQGKPE LKGFNLNPLN QDELKALKVI LKG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Pleckstrin Homology Domain Containing Family F Member 2 Human Recombinant

EAPF, PHAFIN2, ZFYVE18, Pleckstrin homology domain-containing family F member 2, PH domain-containing family F member 2, Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains, PH and FYVE domain-containing protein 2, Zinc finger FYVE domain-containing protein 18, PLEKHF2.

Product # :

PRO-1874

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Description

PLEKHF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-249 a.a) and having a molecular mass of 30.2kDa. PLEKHF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PLEKHF2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Pleckstrin Homology Domain Containing Family F Member 2, also known as PLEKHF2, contains 1 FYVE-type zinc finger and 1 PH domain. PLEKHF2 takes part in early endosome fusion upstream of RAB5, regulates receptor trafficking and fluid-phase transport. PLEKHF2 increases cellular sensitivity to TNF-induced apoptosis.
Synonyms
EAPF, PHAFIN2, ZFYVE18, Pleckstrin homology domain-containing family F member 2, PH domain-containing family F member 2, Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains, PH and FYVE domain-containing protein 2, Zinc finger FYVE domain-containing protein 18, PLEKHF2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVDRLAN SEANTRRISI VENCFGAAGQ PLTIPGRVLI GEGVLTKLCR KKPKARQFFL FNDILVYGNI VIQKKKYNKQ HIIPLENVTI DSIKDEGDLR NGWLIKTPTK SFAVYAATAT EKSEWMNHIN KCVTDLLSKS GKTPSNEHAA VWVPDSEATV CMRCQKAKFT PVNRRHHCRK CGFVVCGPCS EKRFLLPSQS SKPVRICDFC YDLLSAGDMA TCQPARSDSY SQSLKSPLND MSDDDDDDDS SD.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Transforming Growth Factor-Beta 1 Mouse Recombinant, CHO

Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.

Product # :

CYT-1264

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Description

Transforming Growth Factor-Beta 1 Mouse Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa.
TGFB1 Mouse Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

The biological activity was determined by TGFB1 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

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Synonyms
Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 1 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Transforming Growth Factor-Beta 1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSALDTNYC FSSTEKNCCV RQLYIDFRKD LGWKWIHEPK GYHANFCLGP CPYIWSLDTQ YSKVLALYNQ HNPGASASPC CVPQALEPLP IVYYVGRKPK VEQLSNMIVR SCKCS.
Background
Mouse TGF-β1 as an inducer of EMT [epithelial–mesenchymal transition ] therefore used in in fibrosis, wound healing, cancer invasion, and metastasis. Mouse TGF-β1 decreases E-cadherin expression and increases N-cadherin, vimentin and fibronectin.
TGF-β1 is produced by T regulatory cells (Tregs), Macrophages and monocytes, Platelets, Fibroblasts, Epithelial cells, Endothelial cells, Smooth muscle cells, Tumor cells, Activated immune cells
What is the source or expression system of Mouse TGFB1 Protein?
CHO Cells

What is the Purity of Mouse TGFB1 Protein?
Mouse TGFB1 Protein is >97% pure as determined by SDS-PAGE and SEC-HPLC analyses.

What is the molecular weight of Mouse TGFB1 Protein?
Mouse TGFB1 Protein having a total Mw of 25.6kDa.

What is the Biological Activity of Mouse TGFB1 Protein?
The biological functionality of Mouse TGFB1 Protein is determined by mouse HT-2 cells.

What is the endotoxin level for Mouse TGFB1 Protein?
The endotoxin level is minimal, Mouse TGFB1 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of Mouse TGFB1 Protein?
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASASPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.

Is TGFB1 a homodimer / homodimeric protein?
Yes, TGFB1 is homo dimer consisting of 2 identical chains.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor Mouse Recombinant, His Tag

Urogastrone, URG, EGF.

Product # :

CYT-138

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SDS-PAGE

Description

EGF mouse Recombinant produced in E. coli is a single polypeptide chain containing 77 amino acids (977-1029) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EGF solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
Background
Unveiling Epidermal Growth Factor Mouse Recombinant: Harnessing His Tag for Enhanced Insights and Therapeutic Prospects
Abstract:
This research paper delves into the realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), focusing on the strategic integration of a Histidine (His) Tag. By employing sophisticated methodologies encompassing protein engineering, chromatographic techniques, and cellular assays, this study unveils the multifaceted molecular attributes of EGF-MR with His Tag. The findings not only enhance our understanding of EGF-MR's behavior but also illuminate potential avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) governs vital cellular processes. This paper delves into Epidermal Growth Factor Mouse Recombinant (EGF-MR) with a specific emphasis on the incorporation of a Histidine (His) Tag, unraveling its molecular intricacies and therapeutic implications.
Protein Engineering and His Tag Integration:
The paper navigates the tailored engineering of EGF-MR to accommodate a His Tag, a peptide sequence that facilitates protein purification. The process involves strategic modification of the EGF-MR gene to ensure proper folding and presentation of the His Tag.
Chromatographic Purification and His Tag Affinity:
Chromatographic techniques, specifically immobilized metal ion affinity chromatography (IMAC), are employed to purify the His-tagged EGF-MR. The His Tag's high affinity for metal ions facilitates efficient purification, yielding a highly purified and bioactive protein product.
Structural and Functional Insights:
The presence of the His Tag is not just for purification; it serves as a molecular handle to investigate EGF-MR's structural dynamics. High-resolution structural analyses coupled with biophysical assays unravel how the His Tag affects EGF-MR's conformation and binding interactions.
Cellular Assays and Bioactivity Assessment:
In vitro cellular assays, including proliferation and migration studies, provide insights into the impact of His Tag on EGF-MR's bioactivity. Comparative analyses shed light on the functionality of His-tagged EGF-MR and its potential implications in cellular responses.
Therapeutic Prospects and Targeted Delivery:
The incorporation of a His Tag presents a unique avenue for tailored drug delivery. The His Tag can serve as a docking site for targeted therapies, enabling precise interactions with specific receptors on target cells.
Future Directions and Challenges:
While promising, challenges such as potential steric hindrance from the His Tag require consideration. Future research should focus on optimizing the positioning of the His Tag to maintain EGF-MR's full biological activity.
Conclusion:
In a harmonious synthesis of advanced methodologies and innovative insights, the integration of His Tag into Epidermal Growth Factor Mouse Recombinant emerges as a transformative paradigm. The His Tag not only facilitates purification but also offers a molecular window into EGF-MR's behavior, potentially redefining targeted therapies and precision medicine.
What is the molecular weight/Mw of EGF MOUSE, HIS Protein?
EGF MOUSE, HIS Protein has a total Mw of 8.6kDa.

What is the source or expression system of EGF MOUSE, HIS Protein?
Escherichia Coli.

What is the Purity of EGF MOUSE, HIS Protein?
EGF MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF MOUSE, HIS Protein?
The biological functionality of EGF MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of EGF MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

What applications can EGF MOUSE, HIS Protein be used in?
EGF MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF MOUSE, HIS Protein?
The endotoxin level is minimal, EGF MOUSE, HIS Protein was purified using conventional chromatography techniques

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Phosphoglycerate Mutase 1 Mouse Recombinant

Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.

Product # :

ENZ-627

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Description

PGAM1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-254) and having a molecular mass of 31.4kDa.PGAM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PGAM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.
Synonyms
Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.
Physical Appearance
Sterile Filtered clear colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAYKL VLIRHGESAW NLENRFSGWY DADLSPAGHE EAKRGGQALR DAGYEFDICF TSVQKRAIRT LWTVLDAIDQ MWLPVVRTWR LNERHYGGLT GLNKAETAAK HGEAQVKIWR RSYDVPPPPM EPDHPFYSNI SKDRRYADLT EDQLPSCESL KDTIARALPF WNEEIVPQIK EGKRVLIAAH GNSLRGIVKH LEGLSEEAIM ELNLPTGIPI VYELDKNLKP IKPMQFLGDE ETVRKAMEAV AAQGKVKK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Phosphoglycerate Mutase 1 Mouse Recombinant, Active

Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.

Product # :

ENZ-980

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Description

PGAM1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-254) and having a molecular mass of 31.4kDa.PGAM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PGAM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Specific activity is >150units/mg, in which One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37C.

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Introduction
PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.
Synonyms
Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.
Physical Appearance
Sterile Filtered clear colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAYKL VLIRHGESAW NLENRFSGWY DADLSPAGHE EAKRGGQALR DAGYEFDICF TSVQKRAIRT LWTVLDAIDQ MWLPVVRTWR LNERHYGGLT GLNKAETAAK HGEAQVKIWR RSYDVPPPPM EPDHPFYSNI SKDRRYADLT EDQLPSCESL KDTIARALPF WNEEIVPQIK EGKRVLIAAH GNSLRGIVKH LEGLSEEAIM ELNLPTGIPI VYELDKNLKP IKPMQFLGDE ETVRKAMEAV AAQGKVKK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Phosphoglycerate Mutase 2 Human Recombinant

Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.

Product # :

ENZ-578

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Description

PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PGAM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.
Synonyms
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth differentiation factor 5 Human Recombinant, His Tag

Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.

Product # :

CYT-653

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Description

GDF5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (382-501 a.a.) and having a total molecular mass of 15.8 kDa. GDF5 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF5 solution contains 10mM sodium citrate pH-3.5 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
Synonyms
Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.
Background
What is the molecular weight/Mw of GDF5 HUMAN, HIS Protein?
GDF5 HUMAN, HIS Protein has a total Mw of 15.8kDa.

What is the source or expression system of GDF5 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF5 HUMAN, HIS Protein?
GDF5 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF5 HUMAN, HIS Protein?
The biological functionality of GDF5 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GDF5 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.

What applications can GDF5 HUMAN, HIS Protein be used in?
GDF5 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF5 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF5 HUMAN, HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Transforming Growth Factor-Beta 3 Human Recombinant, Plant

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-588

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

TGFB3 Human Recombinant produced in plant is a disulfide-linked homodimeric, glycosylated, polypeptide chain containing 118 amino acids and having a molecular mass of 27.2kDa. The TGFB3 is fused to 6xHis tag at N-terminus and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The biological activity of TGFB3 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 ? 40ng/ml corresponding to a specific activity of 25,000 Units/mg.

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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TGFB3 in sterile 5mM HCl & 50ug/ml BSA at a concentration of 0.05mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKG
YYANFCSGPCPYLRSADTTHSTVLGLY
NTLNPEASASP
CCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Beta-Nerve Growth Factor Human Recombinant, CHO

Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

Product # :

CYT-246

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Nerve Growth Factor-beta Human Recombinant produced in CHO is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.The NGF-b is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells.

Formulation

The protein was lyophilized from a 0.2µm filtered solution in 20mM PB and 250mM NaCl, pH 7.0.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 10⁶ units/mg.

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Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Nerve Growth Factor b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Nerve Growth Factor-beta should be stored at 4°C between 2-7 days and for future use below -18°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized NGF-b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Was analyzed by Mass spectrometry.
Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 26.5kDa.

What is the source or expression system of B NGF Protein?
Chinese Hamster Ovary Cells.

What is the Purity of B NGF Protein?
B NGF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of B NGF Protein?
The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.

What is the amino acid sequence of B NGF Protein?
B NGF Protein is composed from 118 amino acids.

What applications can B NGF Protein be used in?
B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for B NGF Protein?
The endotoxin level is minimal, B NGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Transforming Growth Factor-Beta 1 Human Recombinant, HEK

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

Product # :

CYT-1260

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

TGFB1 Human Recombinant produced in 293 cells is a glycosylated homodimer polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.0kDa. The TGFB1 is purified by proprietary chromatographic techniques.

Source

HEK 293 cells.

Formulation

Lyophilized from a sterile filtered solution containing TFA (0.1%).

Purity

Greater than 98.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 10⁷ units/mg.

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Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TGFB1 in sterile in 18MΩ-cm H2O at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
Background
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-8 Human Recombinant

FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

Product # :

CYT-839

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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Description

FGF 8 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile 0.2 micron filtered aqueous solution containing 0.1% TFA.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED₅₀, as determined by its ability to induce proliferation of NR6-R 3T3, is 0.915ng/ml, corresponding to a specific activity of 1.1x10⁶units/mg.

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Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FGF-8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR.
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 22.5kDa.

What is the source or expression system of FGF8 Protein?
Escherichia Coli.

What is the Purity of FGF8 Protein?
FGF8 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF8 Protein?
The ED50, as determined by its ability to induce proliferation of NR6-R 3T3, is 0.915ng/ml, corresponding to a specific activity of 1.1x106units/mg.

What is the amino acid sequence of FGF8 Protein?
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR.

What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Insulin-Like Growth Factor 1 Des (1-3) Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).

Product # :

CYT-518

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IGF-I Des(1-3) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids (aa 4-70) and having a molecular mass of 7368.5 Dalton. IGF-1 Des1-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized was lyophilized from a 0.2µm filtered concentrated solution in 20mM PBS, pH 7.0.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5×10⁵ units/mg.

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF-I des(1-3) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 des-1-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the IGF-I des(1-3) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TLCGAELVDA LQFVCGDRGF YFNKPTGYGS SSRRAPQTGI VDECCFRSCD LRRLEMYCAP LKPAKSA.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cyclophilin-F, Mouse Anti Human

Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

Product # :

ANT-389

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
Synonyms
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
Immunogen
Anti-human Cyclophilin-F mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Cyclophilin-F amino acids 30-207 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT1F5AT.
Applications
Cyclophilin-F antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot is 1:500~1:1,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:500 and Immunohistochemistry is 1:50.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
Cyclophilin-F antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth Hormone Placental 22kDa Human Recombinant

GHL, GHV, GH-V, hGH-V, PGH.

Product # :

CYT-235

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Placental HGH 22kDa Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 22367 Dalton. Predicted pI=7.80. Placental Growth Hormone has dimished lactogenic (prolactin receptor mediated) activity characteristic to pituitary GHs. GH Placental Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3 previously adjusted pH 8-9.

Purity

Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GHL, GHV, GH-V, hGH-V, PGH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH placental although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization HGH placental can be stored at 4°C for up to 4 weeks. For long term storage and more diluted solutions it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Placental HGH in 0.4% NaHCO3or water adjusted to pH 9, not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Phe-Pro-Thr-Ile.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.18 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GH-22K-placental as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor Human Recombinant

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-241

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38.2kDa.The VEGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The VEGF protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 3.7-5.6 ng/ml, corresponding to a Specific Activity of 178,570-270,270IU/mg.

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Introduction
Vascular endothelial growth factor (VEGF) is an important signaling protein involved in vessel formation As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces vasculogenesis and endothelial cell production, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. VEGF is located in normal cartilage though only osteoarthritic cartilage expresses the VEGF receptors, NP1, VEGFR1 and VEGFR2. The VEGF level in the culture media from OA chondrocytes was more than 3 folds higher than in media from normal chondrocytes
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized VEGF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR
Protein content
VEGF protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.2875 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of VEGF as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

IGF-1 Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.

Product # :

CYT-216

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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purity
biological activity
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Description

IGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.6kDa.IGF-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated solution in PBS, pH 7.0.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 10⁵IU/mg.

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Introduction
The somatomedins, IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B.
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IGF-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
Background
IGF stands for INS like growth factors, which are proteins that have a high similarity to INS. They are part of a complicated process that uses cells to communication with the physiologic environment around them. IGF’s complex system is often called the ‘axis’. This consists of:
● Two cell-surface receptors (IGF1R and IGF2R)
● Two ligands (IGF-1 and IGF-2)
● A family of six high-affinity IGF-binding proteins.
● Proteases.
The Effect IGF Has On The Body
Many unique tissue types express the IGF-1 receptor, and the effects can vary. It induces the survival of neurons, may catalyse skeletal muscle hypertrophy by inducing protein synthesis, and by blocking muscle atrophy. It works as a protector for cartilage cells, and may work to be an anabolic factor for the bones. When used in high concentrations, it can activate the INS receptor, and can even complement the effects that INS has on the body.
Diseases And IGF
Diseases and IGF are closely related, and a number of them can be affected. The INS IGF axis is thought to have an effect on aging, with an increased life span shown in fruit flies when used in studies.
It is also important to note the crucial role that IGF plays in cancer and diabetes - IGF- 1 has been shown to stimulate growth in both prostate and breast cancer cells. The degree of risk that IGF-1 poses is up for debate, and many scientists are not in agreement. IGF has also shown to have the ability to decrease blood glucose levels, although not quite as effective as INS.
How Was IGF Discovered?
Investigators began studying the effects of biological substances on cells and tissues outside the body when IGFs were discovered. The name is self explanatory in the fact that IGF performs INS actions in some tissues, but is less potent than INS at decreasing blood sugar. Its fundamental action is to stimulate growth, whether that be within the epidermal growth factor or the nerve growth factor.
What’s The Difference Between IGF-1 And IGF-2?
The two types of IGF are IGF-1 and IGF-2. Although the names are similar, the specific actions that they take are different - they bind and activate completely difference receptors. The major actor in them both is the effect that they have on cell growth. Most of the actions of the pituitary GH are mediated by IGFs, but predominantly IGF-1. GH works to stimulate many tissues within the body, especially the liver which then secretes IGF-1. This then causes hypertrophy, or in layman's terms, an increase in cell size, as well as hyperplasia which is an increase in the number of cells.
The IGF-1 concentration will increase during childhood and hit peak during puberty, but will then decrease afterwards, as does the hormone secretion itself. It has been proven that children and adults with a deficiency of the GH have low serum IGF-1 concentrations when put in comparison with others in the same age range. Patients who have conditions like acromegaly have been shown to have increased serum IGF-1 concentrations. The production of IGF-2 is less dependent on the secretion of GH than IGF-1, and is much less important for stimulating linear growth.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-18 Human Recombinant, His Tag

Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

Product # :

CYT-935

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source
formulation
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Description

FGF18 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu28-Ala207) containing 190 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 22.3kDa.

Source

Escherichia Coli.

Formulation

FGF18 was filtered (0.4µm) and lyophilized in phosphate buffered saline and 5% w/v trehalose.

Purity

Purity as determined by densitometric image analysis is greater than 95%.

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Introduction
Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.
Synonyms
Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. FGF18 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.
Background
What is the molecular weight/Mw of FGF18 HIS Protein?
FGF18 HIS Protein has a total Mw of 22.3kDa.

What is the source or expression system of FGF18 HIS Protein?
Escherichia Coli.

What is the Purity of FGF18 HIS Protein?
FGF18 HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF18 HIS Protein?
The biological functionality of FGF18 HIS Protein will be determined in the future.

What is the amino acid sequence of FGF18 HIS Protein?
MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.

What applications can FGF18 HIS Protein be used in?
FGF18 HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF18 HIS Protein?
The endotoxin level is minimal, FGF18 HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth and Differentiation factor 11 Human Recombinant

Growth Differentiation Factor 11, GDF-11, Bone Morphogenetic Protein 11, BMP11.

Product # :

CYT-402

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Shipped at Room temp

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source
formulation
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biological activity
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Description

GDF11 Human Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2x109 amino acids and having a total molecular mass of 25kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50, determined by the ability to inhibit alkaline phosphatase activity in ATDC5 cells, is typically less than 1 ng/mL. This corresponds to a specific activity of 1x106 units/mg.

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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
Synonyms
Growth Differentiation Factor 11, GDF-11, Bone Morphogenetic Protein 11, BMP11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF11 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GDF11 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NLGLDCDEHS SESRCCRYPL TVDFEAFGWD WIIAPKRYKA NYCSGQCEYM FMQKYPHTHLVQQANPRGSA GPCCTPTKMS PINMLYFNDK QQIIYGKIPG MVVDRCGCS
Background
What is the molecular weight/Mw of GDF11 HUMAN Protein?
GDF11 HUMAN Protein has a total Mw of 25kDa.

What is the source or expression system of GDF11 HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF11 HUMAN Protein?
GDF11 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF11 HUMAN Protein?
The ED50, determined by the ability to inhibit alkaline phosphatase activity in ATDC5 cells, is typically less than 1 ng/mL. This corresponds to a specific activity of 1x106 units/mg.
What is the amino acid sequence of GDF11 HUMAN Protein?
NLGLDCDEHS SESRCCRYPL TVDFEAFGWD WIIAPKRYKA NYCSGQCEYM FMQKYPHTHL
VQQANPRGSA GPCCTPTKMS PINMLYFNDK QQIIYGKIPG MVVDRCGCS.

What applications can GDF11 HUMAN Protein be used in?
GDF11 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF11 HUMAN Protein?
The endotoxin level is minimal, GDF11 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-6 Human Recombinant

Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.

Product # :

CYT-979

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Shipped at Room temp

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source
formulation
purity
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Description

FGF6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 169 amino acids and having a molecular mass of 18.9kDa.The FGF-6 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-6 protein was lyophilized from a 0.2µm filtered solution in 10mM sodium phosphate and 50mM sodium chloride pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Fibroblast Growth Factor-6 (FGF6) belongs to the fibroblast growth factor (FGF) family. FGF family members possess extensive mitogenic and cell survival functions, and are involved in various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF6 gene displayes oncogenic transforming activity when transfected into mammalian cells. The mouse homolog of the FGF6 gene displays a restricted expression profile predominantly in the myogenic lineage, suggesting a role in muscle regeneration or differentiation.
Synonyms
Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-6 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FGF6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.
Background
What is the molecular weight/Mw of FGF6 Protein?
FGF6 Protein has a total Mw of 18.9kDa.

What is the source or expression system of FGF6 Protein?
Escherichia Coli.

What is the Purity of FGF6 Protein?
FGF6 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF6 Protein?
The biological functionality of FGF6 Protein will be determined in the future.

What is the amino acid sequence of FGF6 Protein?
MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.

What applications can FGF6 Protein be used in?
FGF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF6 Protein?
The endotoxin level is minimal, FGF6 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Amphiregulin Human Recombinant

Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.

Product # :

CYT-041

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Quantity :

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Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Amphiregulin (AREG) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.3 KDa.The AREG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED₅₀ for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

More Info

Synonyms
Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized AREG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AREG should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized AREG in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.
Background
Amphiregulin Human Recombinant: Exploring its Role in Cancer Biology and Therapeutic Applications
Abstract:

Amphiregulin, a member of the epidermal growth factor (EGF) family, has gained significant attention in cancer research. This research paper provides an overview of Amphiregulin human recombinant, highlighting its molecular characteristics, signaling pathways, and therapeutic potential. Understanding the multifaceted role of Amphiregulin opens avenues for targeted cancer therapies. This article provides a concise analysis of Amphiregulin, emphasizing its impact on cancer biology and its therapeutic applications.
Introduction:

Cancer continues to be a significant health challenge worldwide, necessitating novel therapeutic approaches. Amphiregulin, an EGF family member, has emerged as a promising target in cancer research. This paper provides an overview of Amphiregulin, shedding light on its structure, function, and therapeutic potential.
Amphiregulin Signaling and Mechanisms:

Amphiregulin exerts its effects through the binding and activation of the EGF receptor (EGFR). Upon activation, a cascade of intracellular signaling pathways is triggered, including the MAPK and PI3K/AKT pathways. These pathways regulate critical cellular processes such as cell proliferation, survival, migration, and angiogenesis.
Amphiregulin in Cancer Biology:

Amphiregulin has been implicated in various aspects of cancer biology, including tumor growth, metastasis, and resistance to therapy. Its overexpression is observed in several cancer types, and its role in promoting tumor growth and metastasis has been demonstrated in preclinical studies. Targeting Amphiregulin signaling shows promise in inhibiting cancer progression and overcoming therapy resistance.
Therapeutic Potential of Amphiregulin Human Recombinant:

Amphiregulin human recombinant holds significant therapeutic potential in cancer treatment. Strategies aimed at blocking Amphiregulin-EGFR interactions or inhibiting downstream signaling pathways are being explored as potential therapeutic interventions. Additionally, Amphiregulin could serve as a predictive biomarker to identify patients who are more likely to respond to targeted therapies.
Challenges and Future Directions:

While the therapeutic targeting of Amphiregulin shows promise, several challenges need to be addressed. Further research is required to fully understand the complex interplay between Amphiregulin and other molecular pathways in cancer biology. Additionally, the development of specific and potent inhibitors and the identification of patient selection criteria are important considerations for successful clinical translation.
Conclusion:

Amphiregulin human recombinant represents a promising avenue for targeted cancer therapy. Understanding the molecular mechanisms and functional implications of Amphiregulin in cancer biology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve patient outcomes and contribute to the advancement of personalized medicine.
What is the molecular weight/Mw of AREG Protein?
AREG Protein has a total Mw of 11.3kDa.

What is the source or expression system of AREG Protein?
Escherichia Coli.

What is the Purity of AREG Protein?
AREG Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of AREG Protein?
Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

What is the amino acid sequence of AREG Protein?
SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

What applications can AREG Protein be used in?
AREG Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AREG Protein?
The endotoxin level is minimal, AREG Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-5 Human Recombinant

Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.

Product # :

CYT-957

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
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Description

FGF5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 252 amino acids and having a molecular mass of 27.7kDa.The FGF-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-5 protein was lyophilized from a 0.2µm filtered solution in 10mM sodium phosphate and 100mM sodium chloride pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Fibroblast Growth Factor-5 (FGF5) belongs to the FGF family of mitogenic peptides. In vitro, rhFGF5 is a mitogen for Balb/3T3 fibroblasts and bovine heart endothelial cells. FGF5 is also a major muscle-derived survival factor for cultured spinal motoneurons. In vivo, FGF5 is assumed to play central roles in both embryology and neurobiology. Developmentally, FGF5 mRNA is originally found in the embryoblast followed by the lateral somatic mesoderm, where it may play a part in angiogenesis, as well as the myotomes cranial to the tail region, where it may delay terminal myoblast differentiation during cell migration.
Synonyms
Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-5 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FGF5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAWAHGEKRL APKGQPGPAA TDRNPRGSSS RQSSSSAMSS SSASSSPAAS LGSQGSGLEQ SSFQWSPSGR RTGSLYCRVG IGFHLQIYPD GKVNGSHEAN MLSVLEIFAV SQGIVGIRGV FSNKFLAMSK KGKLHASAKF TDDCKFRERF QENSYNTYAS AIHRTEKTGR EWYVALNKRG KAKRGCSPRV KPQHISTHFL PRFKQSEQPE LSFTVTVPEK KKPPSPIKSK IPLSAPRKNT NSVKYRLKFR FG.
Background
What is the molecular weight/Mw of FGF5 HUMAN Protein?
FGF5 HUMAN Protein has a total Mw of 27.7kDa.

What is the source or expression system of FGF5 HUMAN Protein?
Escherichia Coli.

What is the Purity of FGF5 HUMAN Protein?
FGF5 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF5 HUMAN Protein?
The biological functionality of FGF5 HUMAN Protein will be determined in the future.

What is the amino acid sequence of FGF5 HUMAN Protein?
MAWAHGEKRL APKGQPGPAA TDRNPRGSSS RQSSSSAMSS SSASSSPAAS LGSQGSGLEQ SSFQWSPSGR RTGSLYCRVG IGFHLQIYPD GKVNGSHEAN MLSVLEIFAV SQGIVGIRGV FSNKFLAMSK KGKLHASAKF TDDCKFRERF QENSYNTYAS AIHRTEKTGR EWYVALNKRG KAKRGCSPRV KPQHISTHFL PRFKQSEQPE LSFTVTVPEK KKPPSPIKSK IPLSAPRKNT NSVKYRLKFR FG.
What applications can FGF5 HUMAN Protein be used in?
FGF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF5 HUMAN Protein?
The endotoxin level is minimal, FGF5 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-acidic (154 a.a.) Human Recombinant

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Product # :

CYT-1112

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Quantity :

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Shipped at Room temp

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biological activity
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Description

Fibroblast Growth Factor-acidic Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids and having a molecular mass of 17.3kDa. The FGF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4, with 0.5mM DTT, 2mM EDTA, and 5 % Trehalose.

Purity

Greater than 97.0% as determined by:

(a) Analysis by RP-HPLC.

(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×10⁶IU/mg in the presence of 10µg/ml Heparin.

More Info

Introduction
Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF1 functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor.FGF1 acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-acidic should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-acidic Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 17.3kDa.

What is the source or expression system of FGF 1 Protein?
Escherichia Coli.

What is the Purity of FGF 1 Protein?
FGF 1 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×106 IU/mg in the presence of 10µg/ml Heparin.

What is the amino acid sequence of FGF 1 Protein?
AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.

What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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