Search: 1000 results found for "trefoil factor"

Description:

Placental Growth Factor-1 Human Recombinant, Sf9

PIGF, PGF, PLGF-1.

Product # :

CYT-419

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Description

Placenta Growth Factor-1 Human Recombinant produced in insect cells is a homodimer, glycosylated polypeptide chain containing 2 x 131 amino acids and having a total molecular mass of approximately 34 kDa. The PLGF-1 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 50mM acetic acid.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by its ability to bind to immobilized rh-sFlt-1 in a functional ELISA. PlGF-1 human Recombinant can bind to immobilized rh-sFlt-1 (100ng/well) with a linear range at 0.5-10ng/ml, corresponding to a Specific Activity of 1x10⁵-2x10⁶units/mg.

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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
Synonyms
PIGF, PGF, PLGF-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Placenta Growth Factor 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF1 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 Placenta Growth Factor 1 in sterile 0.1M acetic acid not less than 100µg/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 Met-Leu-Pro-Ala-Val.

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:

Hepatoma Derived Growth Factor-Like 1 Human Recombinant

Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.

Product # :

CYT-850

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Description

HDGFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-251 a.a) and having a molecular mass of 29.6kDa.HDGFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HDGFL1 protein solution (0.25mg/ml) containing Phosphate buffered saline, (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Hepatoma Derived Growth Factor-Like 1 (HDGFL1) is a member of the HDGF family and contains 1 PWWP domain.
Synonyms
Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.
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 MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.
Background
What is the molecular weight/Mw of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein has a total Mw of 29.6kDa.

What is the source or expression system of HDGFL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of HDGFL1 HUMAN Protein?
The biological functionality of HDGFL1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of HDGFL1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.

What applications can HDGFL1 HUMAN Protein be used in?
HDGFL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HDGFL1 HUMAN Protein?
The endotoxin level is minimal, HDGFL1 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:

Milk Fat Globule-EGF Factor 8 Protein Mouse Recombinant

Milk fat globule-EGF factor 8 protein, isoform CRA_a, Putative uncharacterized protein, Mfge8, mCG_6301.

Product # :

CYT-1000

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Description

MFGE8 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (23-426a.a.) and having a molecular mass of 46kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MFGE8 is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

MFGE8 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Milk fat globule-EGF factor 8 protein (Mfge8) is pleiotropic secreted glycoprotein which promotes mammary gland morphogenesis, angiogenesis, and tumor progression. Mfge8 has also an imperative role in tissue homeostasis and the prevention of inflammation. Mfge8 functions as a bridge between phosphatidylserine on apoptotic cells and Integrin alpha V beta 3 on phagocytes, leading to the clearance of apoptotic debris.
Synonyms
Milk fat globule-EGF factor 8 protein, isoform CRA_a, Putative uncharacterized protein, Mfge8, mCG_6301.
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
ADLASGDFCD SSLCLNGGTC LTGQDNDIYC LCPEGFTGLV CNETERGPCS PNPCYNDAKC LVTLDTQRGD IFTEYICQCP VGYSGIHCET GCSTQLGMEG GAIADSQISA SSVYMGFMGL QRWGPELARL YRTGIVNAWT ASNYDSKPWI QVNLLRKMRV SGVMTQGASR AGRAEYLKTF KVAYSLDGRK FEFIQDESGG DKEFLGNLDN NSLKVNMFNP TLEAQYIKLY PVSCHRGCTL RFELLGCELH GCSEPLGLKN NTIPDSQMSA SSSYKTWNLR AFGWYPHLGR LDNQGKINAW TAQSNSAKEW LQVDLGTQRQ VTGIITQGAR DFGHIQYVAS YKVAHSDDGV QWTVYEEQGS SKVFQGNLDN NSHKKNIFEK PFMARYVRVL PVSWHNRITL RLELLGCHHH HHH.
Background
An Insight into Milk Fat Globule-EGF Factor 8 Protein (Mouse Recombinant): Characteristics, Applications, and Future Directions
Abstract
The Milk Fat Globule-EGF Factor 8 (MFG-E8) protein, particularly in its mouse recombinant form, has emerged as a pivotal player in multiple physiological processes. This paper aims to elucidate its unique characteristics, delve into current methodologies employed in its study, and chart the trajectory for future research directions.
Introduction
Milk Fat Globule-EGF Factor 8 (MFG-E8) is a glycoprotein known for its vital role in several cellular processes, including cell signaling, apoptosis, and phagocytosis. The recombinant form of MFG-E8 derived from mouse models offers a valuable tool for researchers in deciphering its biological relevance.
Characteristics of MFG-E8 (Mouse Recombinant)
1. Structural Profile: The MFG-E8 protein harbors EGF-like domains, which enable its participation in numerous cellular signaling events.
2. Expression Spectrum: While originally identified in mammary epithelial cells, its expression spectrum extends to macrophages, dendritic cells, and other tissues.
3. Biochemical Activity: It plays a key role in facilitating the phagocytic clearance of apoptotic cells by bridging these cells to phagocytes.
Methodologies Employed in MFG-E8 Research
1. Production of Recombinant MFG-E8: Using bacterial expression systems, such as E. coli, mouse MFG-E8 DNA is introduced, followed by protein purification techniques like gel filtration chromatography.
2. Assays: The phagocytosis assays employing fluorescently tagged apoptotic cells and phagocytes enable researchers to quantify MFG-E8's effectiveness in apoptotic cell clearance.
3. Immunoblotting: Through SDS-PAGE and Western blotting, the expression and purification of MFG-E8 can be monitored and validated.
4. Knockout Models: MFG-E8 knockout mice models help decipher its in vivo significance, especially concerning its immune-regulatory roles.
Original Ideas & Implications
The potential for MFG-E8, particularly in its mouse recombinant form, to serve as a therapeutic agent in autoimmune disorders remains a tantalizing prospect. Considering its role in apoptotic cell clearance, dysregulation in MFG-E8 might be implicated in the etiology of autoimmune disorders. Thus, targeting this protein therapeutically may pave the way for innovative treatments.
Conclusions & Future Directions
While the recombinant MFG-E8 protein has elucidated much about the biological implications of this protein, the horizon is rife with potential. Future research might focus on its therapeutic potential, particularly in autoimmunity and inflammation.

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:

Ectodysplasin A Receptor Human Recombinant, Sf9

Ectodysplasin A Receptor, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Downless Homolog, EDA-A1 Receptor, DL, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, Ectodysplasin-A Receptor, ECTD10A, ECTD10B, EDA-A1R, EDA1R, ED1R, EDA3, HRM1, ED5, ED3.

Product # :

PRO-2510

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Description

EDAR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (27-187a.a.) and having a molecular mass of 45.6kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).EDAR is expressed with a 249 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

EDAR protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.
Synonyms
Ectodysplasin A Receptor, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Downless Homolog, EDA-A1 Receptor, DL, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, Ectodysplasin-A Receptor, ECTD10A, ECTD10B, EDA-A1R, EDA1R, ED1R, EDA3, HRM1, ED5, ED3.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
ADPEYSNCGE NEYYNQTTGL CQECPPCGPG EEPYLSCGYG TKDEDYGCVP CPAEKFSKGG YQICRRHKDC EGFFRATVLT PGDMENDAEC GPCLPGYYML ENRPRNIYGM VCYSCLLAPP NTKECVGATS GASANFPGTS GSSTLSPFQH AHKELSGQGH LATAAAAFES ACSLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

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 Human Recombinant

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

Product # :

CYT-264

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Description

Fibroblast Growth Factor-acidic Human Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of approximately 15.8kDa.The FGF acidic is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing PBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀, calculated by the dose-dependant proliferation of mouse BALB/c 3T3 cells is <0.5 ng/ml, corresponding to a specific activity of > 2,000,000IU/mg.

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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. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It 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 hep-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 Fibroblast Growth Factor-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-a 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 in sterile 18MΩ-cm H2O at 4 degrees Celsius at a concentration of 0.1mg-0.25mg per 1ml. Allow sample to sit for 5 min. at 4 degrees, spin to remove precipitant.
Amino Acid Sequence
MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 15.8kDa.

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 >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50, calculated by the dose-dependant proliferation of mouse BALB/c 3T3 cells is <0.5 ng/ml, corresponding to a specific activity of > 2,000,000IU/mg.

What is the amino acid sequence of FGF 1 Protein?
MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

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.

Description:

Fibroblast Growth Factor-basic (147 a.a.) Bovine Recombinant

HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.

Product # :

CYT-1130

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Description

Fibroblast Growth Factor-basic (147 a.a.) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 147 amino acid and having a molecular mass of approximately 16.5kDa.FGF2 (147) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

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 < 0.1 ng/ml, corresponding to a specific activity of > 1.0 ×10⁷IU/mg.

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Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG (CUG) initiation codons resulting in 5 different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
The heparin-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
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-basic (147 a.a.) 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-basic (147 a.a.) in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYSSWYVALK RTGQYKLGPK TGPGQKAILF LPMSAKS.
Background
What is the molecular weight/Mw of FGF2 (147), BOVINE Protein?
FGF2 (147), BOVINE Protein has a total Mw of 16.5kDa.

What is the source or expression system of FGF2 (147), BOVINE Protein?
Escherichia Coli.

What is the Purity of FGF2 (147), BOVINE Protein?
FGF2 (147), BOVINE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF2 (147), BOVINE Protein?
The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0 ×107IU/mg.

What is the amino acid sequence of FGF2 (147), BOVINE Protein?
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYSSWYVALK RTGQYKLGPK TGPGQKAILF LPMSAKS.

What applications can FGF2 (147), BOVINE Protein be used in?
FGF2 (147), BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF2 (147), BOVINE Protein?
The endotoxin level is minimal, FGF2 (147), BOVINE 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 Bovine

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

Product # :

CYT-613

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Description

Fibroblast Growth Factor-acidic Bovine (FGF-1) purified from Bovine Brain contains a 17 kDa and a 20 kDa polypeptide chain. The 17 kDa peptide is derived from the 20K peptide by restricted proteolysis. (See Jaye et al²). The FGF acidic is purified by proprietary chromatographic techniques.

Source

Bovine Brain.

Formulation

Each 5µg aFGF were lyophilized from 0.5ml solution containing 1mM sodium phosphate, pH 7 after filtration over a low binding membrane.

Purity

Greater than 90%.

Biological Activity

Stimulates growth of bovine capillary endothelial cells by 3-5 fold over 5% calf serum at 10-25ng/ml FGF.

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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. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It 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 aFGF although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution aFGF should be stored at 4°C between 2-3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized aFGF in sterile 50mM Na2HPO4 pH-7, and 0.5% albumin. The Recommended concentration in cell culture: 1-20ng/ml.
Background
What is the molecular weight/Mw of AFGF Protein?
AFGF Protein has a total Mw of 17kDa.

What is the source or expression system of AFGF Protein?
Bovine Brain.

What is the Purity of AFGF Protein?
AFGF Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of AFGF Protein?
Stimulates growth of bovine capillary endothelial cells by 3-5 fold over 5% calf serum at 10-25ng/ml FGF.

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

What is the endotoxin level for AFGF Protein?
The endotoxin level is minimal, AFGF 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:

Pentraxin-3 Human Recombinant

TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

Product # :

PRO-694

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Description

Recombinant Human PTX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (18-381 a.a) and having a molecular mass of 44.4 kDa. PTX3 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PTX3 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by Analysis by SDS-PAGE.

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Introduction
PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.
Synonyms
TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMENS DDYDLMYVNL DNEIDNGLHP TEDPTPCDCG QEHSEWDKLF IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA RPCAPGAPAE ARLTSALDEL LQATRDAGRR LARMEGAEAQ RPEEAGRALA AVLEELRQTR ADLHAVQGWA ARSWLPAGCE TAILFPMRSK KIFGSVHPVR PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL SYQSIVFVVG GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE TGGAESCHIR GNIVGWGVTE IQPHGGAQYV S.

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:

Platelet Derived Growth Factor-BB Equine Recombinant

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

Product # :

CYT-1199

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Description

PDGF-BB Equine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide dimer chain containing 2 x 110 amino acids and having a total molecular mass of 24.8kDa.The PDGF-BB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile (0.2µ) filtered solution containing 10 mM sodium phosphate, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by 3T3 proliferation is ≤ 30 ng/mL, corresponding to a specific activity of ≥ 3.3 x 10^4 units/mg.

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Introduction
PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PDGF-BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-BB 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 PDGF-BB in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSLGSLAVAE PAMIAECKTR TEVFEISRRL IDRTNANFLV WPPCVEVQRC SGCCNNRHVQ CRPTQVQLRP VQVRKIEIVR KKPTFKKATV TLEDHLACKC ETVGAARPVT

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:

CD30 Ligand Receptor Mouse Recombinant

Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1

Product # :

CYT-1165

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Description

TNFRSF8 Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 479 amino acids (19-258 aa) and having a molecular mass of 52.2kDa.TNFRSF8 is fused to a 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF8 protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.
Synonyms
Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1
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
FPTDRPLKTT CAGDLSHYPG EAARNCCYQC PSGLSPTQPC PRGPAHCRKQ CAPDYYVNED GKCTACVTCL PGLVEKAPCS GNSPRICECQ PGMHCCTPAV NSCARCKLHC SGEEVVKSPG TAKKDTICEL PSSGSGPNCS NPGDRKTLTS HATPQAMPTL ESPANDSARS LLPMRVTNLV QEDATELVKV PESSSSKARE PSPDPGNAEK NMTLELPSPG TLPDISTSEN SKEPASTAST LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

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, Biotin

Urogastrone, URG, EGF.

Product # :

CYT-841

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Description

EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.

Source

Escherichia Coli.

Formulation

The protein (0.5mg/ml) solution contains sterile PBS.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x10⁶units/mg.

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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 clear solution.
Stability
Should be stored at 4°C.Please do not freeze.
Amino Acid Sequence
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.
Background
Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential
Abstract:
This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.
Introduction:
Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.
Protein Engineering and Biotin Conjugation:
EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.
Cellular Signaling Amplification:
The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.
Cellular Assays and Functional Responses:
In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.
Tailored Delivery Strategies:
The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.
Regenerative Medicine and Targeted Therapy:
The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.
Future Prospects and Challenges:
While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.
Conclusion:
In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.
What is the molecular weight/Mw of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein has a total Mw of 7kDa.

What is the source or expression system of MEGF, BIOTIN Protein?
Escherichia Coli.

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

What is the Biological Activity of MEGF, BIOTIN Protein?
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

What is the amino acid sequence of MEGF, BIOTIN Protein?
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

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

What is the endotoxin level for MEGF, BIOTIN Protein?
The endotoxin level is minimal, MEGF, BIOTIN 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:

Epidermal Growth Factor Mouse

Urogastrone, URG, EGF.

Product # :

CYT-554

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Quantity :

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Shipped at Room temp

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Description

Epidermal Growth Factor Mouse purified from submaxillary gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.1 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Mouse Submaxillary Gland.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

Purity

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

Biological Activity

The biological activity is measured in a proliferation assay using BALB/MK cells.

More Info

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 White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Illuminating Novel Avenues: Epidermal Growth Factor Mouse Variant in Cellular Dynamics and Therapeutic Prospects
Abstract:
This research paper delves into unexplored dimensions of the Epidermal Growth Factor Mouse Variant (EGF-M), unraveling its intricate molecular attributes, signaling cascades, and therapeutic implications. Employing advanced methodologies encompassing transgenic models, cellular assays, and bioinformatics, this study unveils the nuanced cellular responses elicited by EGF-M. The findings underscore its potential as a therapeutic target for regenerative medicine and cancer interventions.
Introduction:
Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper charts a new course, focusing on the Epidermal Growth Factor Mouse Variant (EGF-M), exploring its distinct molecular properties and therapeutic applications.
Molecular Insights and Receptor Binding:
EGF-M's interaction with the epidermal growth factor receptor (EGFR) initiates a cascade of intracellular events. Molecular dynamics simulations and binding studies decipher the nuances of this interaction, shedding light on structural motifs that drive receptor activation and downstream signaling.
Cellular Signaling and Functional Responses:
EGF-M engages canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) pathway and phosphoinositide 3-kinase (PI3K)/Akt pathway. High-resolution microscopy and phosphoproteomics unveil spatiotemporal dynamics, revealing how EGF-M orchestrates cell proliferation, migration, and survival.
Transgenic Mouse Models and In Vivo Implications:
In transgenic mouse models, EGF-M's impact on tissue regeneration becomes evident. Tailored wound healing assays demonstrate accelerated re-epithelialization and granulation tissue formation, affirming its potential in regenerative medicine. Furthermore, xenograft studies suggest its role in modulating tumor microenvironments, offering prospects for cancer therapy.
Bioinformatics in EGF-M Interactions:
Advanced bioinformatics analyses deepen our understanding of EGF-M's cellular interactions. Molecular docking simulations predict potential binding partners and off-target effects, enhancing our comprehension of its biological scope.
Therapeutic Implications and Future Directions:
EGF-M's distinctive attributes open doors for therapeutic innovation. Exploiting its regenerative potential, it holds promise for chronic wound management and tissue engineering. Moreover, targeted interventions exploiting its role in cancer microenvironments might revolutionize oncology treatments.
Challenges and Prospects:
Despite promising strides, challenges linger, including deciphering cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosage regimens to harness EGF-M's therapeutic potential.
Conclusion:
In a synthesis of intricate molecular insights and transformative therapeutic avenues, Epidermal Growth Factor Mouse Variant emerges as a captivating subject. Its distinctive binding mechanisms and multifaceted cellular orchestration spotlight its potential as a regenerative agent and a cancer therapeutic, propelling medical science into a new era.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.1Da.

What is the source or expression system of EGF Protein?
Mouse Submaxillary Gland.

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

What is the Biological Activity of EGF Protein?
The biological activity is measured in a proliferation assay using BALB/MK cells.

What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.

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

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF 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 Receptor II Human Recombinant

AAT3, FAA3, MFS2, RIIC, LDS1B, LDS2B, TAAD2, TGFR-2, TGFbeta-RII, TGFBR-2, TGF-beta receptor type-2, Transforming growth factor-beta receptor type II, TGF-beta receptor type II, TGF-beta type II receptor, TbetaR-II, TGFBR2.

Product # :

PKA-261

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Description

TGFBR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain encoding 133 amino acids (27-159 a.a.), the extracellular domain of TGFBR2, having a molecular mass of 15.1 kDa.TGFBR2 is purified by proprietary chromatographic techniques

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 μm filtered solution in buffer containing 150mM NaCl & 50mM sodium phosphate buffer pH-7.5.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

In ELISA assay, concentrations 0.5-1µg/ml can be used for TGF-beta measurements

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Introduction
TGFBR2 is part of the Ser/Thr protein kinase family and the TGFB receptor subfamily. TGFBR2 is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 expression is increased in oral squamous cell carcinoma cells. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is decreased by IL-1beta while inducing Sp3 via NFkappaB.
Synonyms
AAT3, FAA3, MFS2, RIIC, LDS1B, LDS2B, TAAD2, TGFR-2, TGFbeta-RII, TGFBR-2, TGF-beta receptor type-2, Transforming growth factor-beta receptor type II, TGF-beta receptor type II, TGF-beta type II receptor, TbetaR-II, TGFBR2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFBR2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFBR2 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 TGFBR2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HVQK SVNNDMIVTD NNGAVKFPQL CKFCDVRFST CDNQKSCMSN CSITSICEKP QEVCVAVWRK NDENITLETV CHDPKLPYHD FILEDAASPK CIMKEKKKPG ETFFMCSCSS DECNDNIIFS EEYNTSNPD

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 receptor-1 Human Recombinant, His Tag

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-354

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Description

FLT1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 298 amino acids fragment (31-328) corresponding to the IgG like domains 1-3 from the mature soluble FLT1 protein, having a total molecular mass of 43kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The FLT1 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FLT1 His-Tag protein is supplied in 1x PBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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. Please avoid freeze thaw cycles.

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:

Stromal Cell-Derived Factor-1 gamma Human Recombinant (CXCL12)

Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.

Product # :

CHM-020

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Quantity :

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Shipped at Room temp

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Description

SDF-1 gamma Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 99 amino acids and having a molecular mass of 11.6kDa.The SDF-1g is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SDF-1g protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1a/CXCL12a and SDF-1b/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SDF-1 gamma 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 SDF-1g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.
Background
What is the molecular weight/Mw of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein has a total Mw of 11.6kDa.

What is the source or expression system of CXCL12 HUMAN GAMMA Protein?
Escherichia Coli.

What is the Purity of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein is > 96% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 HUMAN GAMMA Protein?
The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.

What is the amino acid sequence of CXCL12 HUMAN GAMMA Protein?
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.

What applications can CXCL12 HUMAN GAMMA Protein be used in?
CXCL12 HUMAN GAMMA Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL12 HUMAN GAMMA Protein?
The endotoxin level is minimal, CXCL12 HUMAN GAMMA Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL12 HUMAN GAMMA that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL12 HUMAN GAMMA?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Keratinocyte Growth Factor-2 Human Recombinant

FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.

Product # :

CYT-303

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Quantity :

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Shipped at Room temp

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Description

Keratinocyte Growth Factor-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (40-208) and having a molecular mass of 19300 Dalton. Keratinocyte Growth Factor 2 is highly related to KGF-1(FGF-7), it binds to the same receptor as KGF-1 and shares 57% sequence homology. The FGF10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2um filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by the dose-dependant stimulation of FGF receptors by BaF3 indicator cells (measured by ³H-thymidine uptake) is < 0.5 ng/ml, corresponding to a specific activity of 2x10⁶units/mg.

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Introduction
KGF-2 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. FGF-10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7. Studies of the mouse homolog of suggested that this gene is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of lim bud formation. This gene is also implicated to be a primary factor in the process of wound healing.
Synonyms
FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Keratinocyte Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF10 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-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLGQDMVSPE ATNSSSSSFS SPSSAGRHVR SYNHLQGDVR WRKLFSFTKY FLKIEKNGKV SGTKKENCPY SILEITSVEI GVVAVKAINS NYYLAMNKKG KLYGSKEFNN DCKLKERIEE NGYNTYASFN WQHNGRQMYV ALNGKGAPRR GQKTRRKNTS AHFLPMVVHS.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.79 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 standard solution of FGF-10 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 receptor-2 Human Recombinant, His Tag

KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.

Product # :

PKA-099

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Description

VEGFR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 987 amino acids (20-764a.a) and having a molecular mass of 110.5kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa). VEGFR2 is fused to a 239 amino acids hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

VEGFR2 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation.
Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.
Synonyms
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
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
ADPASVGLPS VSLDLPRLSI QKDILTIKAN TTLQITCRGQ RDLDWLWPNN QSGSEQRVEV TECSDGLFCK TLTIPKVIGN DTGAYKCFYR ETDLASVIYV YVQDYRSPFI ASVSDQHGVV YITENKNKTV VIPCLGSISN LNVSLCARYP EKRFVPDGNR ISWDSKKGFT IPSYMISYAG MVFCEAKIND ESYQSIMYIV VVVGYRIYDV VLSPSHGIEL SVGEKLVLNC TARTELNVGI DFNWEYPSSK HQHKKLVNRD LKTQSGSEMK KFLSTLTIDG VTRSDQGLYT CAASSGLMTK KNSTFVRVHE KPFVAFGSGM ESLVEATVGE RVRIPAKYLG YPPPEIKWYK NGIPLESNHT IKAGHVLTIM EVSERDTGNY TVILTNPISK EKQSHVVSLV VYVPPQIGEK SLISPVDSYQ YGTTQTLTCT VYAIPPPHHI HWYWQLEEEC ANEPSQAVSV TNPYPCEEWR SVEDFQGGNK IEVNKNQFAL IEGKNKTVST LVIQAANVSA LYKCEAVNKV GRGERVISFH VTRGPEITLQ PDMQPTEQES VSLWCTADRS TFENLTWYKL GPQPLPIHVG ELPTPVCKNL DTLWKLNATM FSNSTNDILI MELKNASLQD QGDYVCLAQD RKTKKRHCVV RQLTVLERVA PTITGNLENQ TTSIGESIEV SCTASGNPPP QIMWFKDNET LVEDSGIVLK DGNRNLTIRR VRKEDEGLYT CQACSVLGCA KVEAFFIIEG AQEKTNLELE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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-Basic Human Recombinant, Sf9

Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

Product # :

CYT-365

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Description

Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17353 Dalton.The FGF-basic is purified by proprietary chromatographic techniques.

Source

Baculovirus.

Formulation

The sterile protein solution (0.5mg/ml) contains 20mM Tris pH=7.9, 100mM KCl, 1mM DTT and 20% glycerol.

Purity

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

Biological Activity

The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

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Introduction
Basic 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. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It 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 heparin-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
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Physical Appearance
Sterile Filtered liquid formulation.
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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ala-Gly-Ser-Ile.
Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.3kDa.

What is the source or expression system of FGF 2 Protein?
Baculovirus.

What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

What is the amino acid sequence of FGF 2 Protein?
FGF 2 Protein is composed from155 amino acids.

What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 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:

Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

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

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG 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:

Macrophage Migration Inhibitory Factor Human Recombinant, His Tag C-Terminus

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Product # :

CYT-521

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Quantity :

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Description

MIF human Recombinant, fused to His-tag at C-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chaincontaining 123 amino acidsand having a molecular mass of 13.5 kDa.

Source

Escherichia Coli.

Formulation

Human MIF was lyophilized from a 1mg/ml solution containing PBS pH-7.4.

Purity

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

Biological Activity

Measured by its ability to bind rhCD74 in a functional ELISA.

More Info

Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Physical Appearance
Sterile Filtered lyophilized powder.
Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPC
ALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTF
ALEHHHHHH.

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:

Tripartite Motif Containing 33 Human Recombinant

E3 ubiquitin-protein ligase TRIM33, Ectodermin homolog, RET-fused gene 7 protein, Protein Rfg7, Transcription intermediary factor 1-gamma, TIF1-gamma, Tripartite motif-containing protein 33, TRIM33, KIAA1113, RFG7, TIF1G, ECTO, PTC7, TF1G, TIFGAMMA, TIF1GAMMA.

Product # :

PRO-1506

Price :

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Description

TRIM33 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 124,041 Dalton. TRIM33 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 Insect Cells.

Formulation

TRIM33 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Tripartite Motif Containing 33 (TRIM33) belongs to the tripartite motif family. This motif includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM33 is assumed to be a transcriptional corepressor. TRIM33 functions as an E3 ubiquitin-protein ligase. TRIM33 also promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. In addition, TRIM33 inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Furthermore, TRIM33 has a role in the control of cell proliferation.
Synonyms
E3 ubiquitin-protein ligase TRIM33, Ectodermin homolog, RET-fused gene 7 protein, Protein Rfg7, Transcription intermediary factor 1-gamma, TIF1-gamma, Tripartite motif-containing protein 33, TRIM33, KIAA1113, RFG7, TIF1G, ECTO, PTC7, TF1G, TIFGAMMA, TIF1GAMMA.
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. Avoid multiple freeze-thaw cycles.

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 Rat Recombinant, His Tag

VEGF-A, Vascular permeability factor, VPF, VEGF.

Product # :

CYT-854

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Description

VEGF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (206-325 a.a) and having a molecular mass of 16.7kDa.VEGF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

VEGF protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) and 50% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. 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/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
VEGF-A, Vascular permeability factor, VPF, VEGF.
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 MGSHMAPTTE GEQKAHEVVK FMDVYQRSYC RPIETLVDIF QEYPDEIEYI FKPSCVPLMR CAGCCNDEAL ECVPTSESNV TMQIMRIKPH QSQHIGEMSF LQHSRCECRP KKDRTKPEKC DKPRR

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 Rat Recombinant

Fibroblast growth factor 1, FGF-1, Acidic fibroblast growth factor, aFGF, binding growth factor 1, HBGF-1, Fgf1, Fgfa, HBGF1.

Product # :

CYT-075

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Description

Fibroblast Growth Factor-acidic Rat Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.9 kDa.The FGF acidic is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized at a concentration of 1 mg/ml in 5mM Na2PO4, pH-7.5 and 50mM NaCl.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x10⁶IU/mg.

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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. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It 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
Fibroblast growth factor 1, FGF-1, Acidic fibroblast growth factor, aFGF, binding growth factor 1, HBGF-1, Fgf1, Fgfa, HBGF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Fibroblast Growth Factor-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-a 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 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 15.9kDa.

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 >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

What is the amino acid sequence of FGF 1 Protein?
MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

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.

Description:

LIGHT Mouse Recombinant

Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.

Product # :

CYT-826

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

TNFSF14 Mouse Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids and having a molecular mass of 18.4kDa.

Source

Escherichia Coli.

Formulation

TNFSF14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4.

Purity

Greater than 96.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cytotoxicity assay using human HT-29 cells is less than 2µg/ml, corresponding to a specific activity of > 500 IU/mg in the presence of murine anti-polyHistidine monoclonal antibody and rHuIFN-g.

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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
Synonyms
Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFSF14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFSF14 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 TNFSF14 in sterile 100mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DGGKGSWEKL IQDQRSHQAN PAAHLTGANA SLIGIGGPLL WETRLGLAFL RGLTYHDGAL VTMEPGYYYV YSKVQLSGVG CPQGLANGLP ITHGLYKRTS RYPKELELLV SRRSPCGRAN SSRVWWDSSF LGGVVHLEAG EEVVVRVPGN RLVRPRDGTR SYFGAFMV.

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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