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1000 results found for “glypican”
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Name :
Secretin HumanDescription:
Secretin Human
Product # :
HOR-273Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secretin has a molecular formula of C130H220N44O41, a.a. sequence of H-His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg- Asp-Ser-Ala-Arg-Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 and having an Mw of 3055.4 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Human Secretin stimulates the secretion of bicarbonate by the pancreas and inhibits the production of gastrin and acid production in the stomach. It also potentiates the release of digestive enzymes from the pancreas triggered by cholecystokinin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Secretin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secretin 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.
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Solubility
It is recommended to reconstitute the lyophilized Secretin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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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Description:
Myostatin Propeptide Human Recombinant, HEK
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Product # :
CYT-936Price :
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Shipped with Ice Packs
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Description
Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Arg266) containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa. Myostatin Propetide is fused to a 10 aa C-terminal His tag.
Source
HEK 293.
Formulation
Myostatin Propetide solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
GDF8 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. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
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Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
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Physical Appearance
Filtered colorless solution.
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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.
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Amino Acid Sequence
NENSEQKENV EKEGLCNACT WRQNTKSSRI EAIKIQILSK LRLETAPNIS KDVIRQLLPK APPLRELIDQ YDVQRDDSSD GSLEDDDYHA TTETIITMPT ESDFLMQVDG KPKCCFFKFS SKIQYNKVVK AQLWIYLRPV ETPTTVFVQI LRLIKPMKDG TRYTGIRSLK LDMNPGTGIW QSIDVKTVLQ NWLKQPESNL GIEIKALDEN GHDLAVTFPG PGEDGLNPFL EVKVTDTPKR SRR HHHHHHH 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.
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Name :
Leptin HumanDescription:
Human Leptin
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
Product # :
CYT-683Price :
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Shipped at Room temp
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Description
Leptin Human produced syntheticaly contains 35 amino acids (22-56 a.a.) having a molecular mass of 3950.6 Dalton.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 95.0% as determined by RP-HPLC.
More Info
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Introduction
A 16kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature, should be stored desiccated below -20°C. Reconstituted Leptin is best stored refrigerated at 4°C.
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Solubility
The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.
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Amino Acid Sequence
Val-Pro-Ile-Gln-Lys-Val-Gln-Asp-Asp-Thr-Lys-Thr-Leu-Ile-Lys-Thr-Ile-Val-Thr-Arg-Ile-Asn-Asp-Ile-Ser-His-Thr-Gln-Ser-Val-Ser-Ser-Lys-Gln-Lys.
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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Name :
StreptavidinDescription:
Streptavidin Recombinant
Product # :
PRO-791Price :
Quantity :
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Shipped at Room temp
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Description
Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli. The molecular weight per tetramer is approximately 52kDa.
Source
Escherichia Coli.
Formulation
Lyophilized in 10mM potassium phosphate buffer pH 6.5.
Purity
Greater than 98.0% as determined by SDS-PAGE and HPLC.
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Streptavidin is shipped at ambient temperature, upon arrival store at -20°C.
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Solubility
It is recommended to reconstitute the lyophilized Streptavidin in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLT
GRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGA
EARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS. -
Proteolytic Activity
< 10-3 U/mg protein (Azocoll, 25 °C, 24 h, pH 8.0).
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Specific Activity
> 17U/mg (one unit binds 1 μg D-biotin).
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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Name :
MFGE8 MouseDescription:
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-1000Price :
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Shipped with Ice Packs
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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.
More Info
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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.
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Synonyms
Milk fat globule-EGF factor 8 protein, isoform CRA_a, Putative uncharacterized protein, Mfge8, mCG_6301.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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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.
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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.
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Name :
NKIRAS1 HumanDescription:
NFKB Inhibitor Interacting Ras-Like 1 Human Recombinant
NF-kappa-B inhibitor-interacting Ras-like protein 1, I-kappa-B-interacting Ras-like protein 1, Kappa B-Ras protein 1, KappaB-Ras1, NKIRAS1, KBRAS1.
Product # :
PRO-1039Price :
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Shipped with Ice Packs
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Description
NKIRAS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a) and having a molecular mass of 23.8kDa (Molecular weight on SDS-PAGE will appear higher).NKIRAS1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NKIRAS1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NF-kappa-B inhibitor-interacting Ras-like protein 1 (NKIRAS1) is a member of the small GTPase superfamily. NKIRAS1 is an unusual Ras-like protein which acts as a potent regulator of NF-kappa-B activity by thwarting the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, describing why NFKBIB is more resistant to degradation. NKIRAS1 functions by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB.
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Synonyms
NF-kappa-B inhibitor-interacting Ras-like protein 1, I-kappa-B-interacting Ras-like protein 1, Kappa B-Ras protein 1, KappaB-Ras1, NKIRAS1, KBRAS1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGKGCKVVVC GLLSVGKTAI LEQLLYGNHT IGMEDCETME DVYMASVETD RGVKEQLHLY DTRGLQEGVE LPKHYFSFAD GFVLVYSVNN LESFQRVELL KKEIDKFKDK KEVAIVVLGN KIDLSEQRQV DAEVAQQWAK SEKVRLWEVT VTDRKTLIEP FTLLASKLSQ PQSKSSFPLP GRKNKGNSNS EN.
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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Name :
G CSF Human, HEKDescription:
Granulocyte-Colony Stimulating Factor Human Recombinant, HEK
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-088Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
G-CSF Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 21-25kDa due to glycosylation.The G-CSF is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The G-CSF was lyophilized from 1mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells (Mouse Myeloid Leukemia indicator cell line), the ED50 is <0.01ng/ml.
More Info
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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 the GCSF 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.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution G-CSF 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.
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Solubility
It is recommended to reconstitute the lyophilized G-CSF in sterile 1xPBS containing 0.1% endotoxin-free recombinant HSA.
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Background
What is the molecular weight/Mw of G CSF HUMAN, HEK Protein?
G CSF HUMAN, HEK Protein has a total Mw of 23kDa.
What is the source or expression system of G CSF HUMAN, HEK Protein?
HEK.
What is the Purity of G CSF HUMAN, HEK Protein?
G CSF HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF HUMAN, HEK Protein?
The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells (Mouse Myeloid Leukemia indicator cell line), the ED50 is <0.01ng/ml.
What applications can G CSF HUMAN, HEK Protein be used in?
G CSF HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF HUMAN, HEK Protein?
The endotoxin level is minimal, G CSF HUMAN, HEK 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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Name :
Leptin DogDescription:
Leptin Dog Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-506Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Dog Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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.
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Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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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Name :
Cyclophilin F Rat BioactiveDescription:
Cyclophilin-F Rat Recombinant Bioactive
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.
Product # :
ENZ-1019Price :
Quantity :
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Shipped with Ice Packs
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Description
Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206 a.a) and having a molecular mass of 21.2Da. Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cyclophilin F protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,300 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmol of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.More Info
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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.
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Synonyms
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSCSDGGAR GANSSSQNPL VYLDVGADGQ PLGRVVLELK ADVVPKTAEN FRALCTGEKG FGYKGSTFHR VIPAFMCQAG DFTNHNGTGG KSIYGSRFPD ENFTLKHVGP GVLSMANAGP NTNGSQFFIC TIKTDWLDGK HVVFGHVKEG MDVVKKIESF GSKSGKTSKK IVITDCGQLS.
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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Name :
Y.Enterocolitica (O:8) YopMDescription:
Yersinia Enterocolitica (O:8) YopM Recombinant
Product # :
PRO-2272Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Yersinia Enterocolitica (O:8) YopM produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 60,898 Dalton. Y.Enterocolitica (O:8) YopM is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Y.Enterocolitica(O:8) YopM is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Immunological Functions
1. Binds IgG- and IgM- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.
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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Name :
VEGF (121 a.a.) HumanDescription:
Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-343Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.
More Info
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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
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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.
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Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor -121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR R
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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Name :
VTN Human, Sf9Description:
Vitronectin Human Recombinant, Sf9
VN, S-protein, Serum-spreading factor, V75, VTN.
Product # :
pro-2594Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VTN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 468 amino acids (20-478a.a.) and having a molecular mass of 53.3kDa.VTN is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
VTN 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.
Biological Activity
Measured by the ability of the immobilized protein to support the adhesion of B16-F10 mouse melanoma cells. The ED50 is 5ug/ml when cells are added to VTN coated plates.
More Info
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Introduction
Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.
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Synonyms
VN, S-protein, Serum-spreading factor, V75, VTN.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPDQESCKG RCTEGFNVDK KCQCDELCSY YQSCCTDYTA ECKPQVTRGD VFTMPEDEYT
VYDDGEEKNN ATVHEQVGGP SLTSDLQAQS KGNPEQTPVL KPEEEAPAPE VGASKPEGID
SRPETLHPGR PQPPAEEELC SGKPFDAFTD LKNGSLFAFR GQYCYELDEK AVRPGYPKLI
RDVWGIEGPI DAAFTRINCQ GKTYLFKGSQ YWRFEDGVLD PDYPRNISDG FDGIPDNVDA
ALALPAHSYS GRERVYFFKG KQYWEYQFQH QPSQEECEGS SLSAVFEHFA MMQRDSWEDI
FELLFWGRTS AGTRQPQFIS RDWHGVPGQV DAAMAGRIYI SGMAPRPSLA KKQRFRHRNR
KGYRSQRGHS RGRNQNSRRP SRATWLSLFS SEESNLGANN YDDYRMDWLV PATCEPIQSV
FFFSGDKYYR VNLRTRRVDT VDPPYPRSIA QYWLGCPAPG HLHHHHHH.
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.
- View Data Sheet
Name :
SRSF1 Human, Sf9Description:
Serine/arginine-Rich Splicing Factor 1 Human Recombinant, Sf9
SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 2.
Product # :
PRO-2417Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SRSF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (1-248) and having a molecular mass of 28.5kDa. SRSF1 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SRSF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 100mM KCl, 1mM DTT, 0.2mM EDTA and 40% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Serine/arginine-rich splicing factor 1 (SFRS1) belongs to the arginine/serine-rich splicing factor protein family, and functions in both constitutive and alternative pre-mRNA splicing. SFRS1 binds to pre-mRNA transcripts and components of the spliceosome, and can either initiate or inhibit splicing depending on the position of the pre-mRNA binding site. The ability of SFRS1 to activate splicing is controlled by phosphorylation and interactions with other splicing factor associated proteins.
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Synonyms
SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 2.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRTHH HHHH.
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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Name :
SCF Human, HEKDescription:
Stem Cell Factor Human Recombinant, HEK
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Product # :
CYT-111Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SCF Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 35-45kDa due to glycosylation.The SCF is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
SCF was lyophilized from a 0.2µm filtered solution (1mg/ml) containing 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line).
The EC50 is 15.25ng/ml.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
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Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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.
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Solubility
It is recommended to reconstitute the lyophilized SCF in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
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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Name :
Borrelia OspCDescription:
Borrelia Burgdorferi Outer Surface Protein C Recombinant
Product # :
BOR-004Price :
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Shipped with Ice Packs
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Description
Recombinant Borrelia Burgdorferi Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 26kDa. Borrelia OspC is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia OspC is supplied in 16mM HEPES buffer pH-7.0, 300mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Applications
Western blot with Lyme positive plasma.
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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Name :
Shiga Like Toxin 1Description:
Shiga Like Toxin-1 Subunit B Recombinant
Product # :
STX-001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Shiga Like Toxin-1 Subunit B is produced from E.Coli O157:H7 amino acids 2-90 of the Shiga Like Toxin-1 Subunit B.The Shiga Like Toxin 1 protein is fused to a 6xHis tag at its N-terminus and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
Phosphate buffered saline and 25mM K₂CO₃.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
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Introduction
Shiga-like toxin (verotoxin) is a toxin produced by some strains of Escherichia coli. Shiga-like toxin is named for its similarity to the AB5-type Shiga toxin produced by the bacteria Shigella dysenteriae. There are two known types-SLT1 and SLT2. The Shiga-like toxin is linked with hemolytic-uremic syndrome. Shiga-like toxin requires highly specific receptors on the cells' surface in order to attach and enter the cell. Species such as cattle, swine, and deer which do not carry these receptors may harbor toxigenic bacteria without any ill effect, dropping them in their feces, from where they may be distributed to humans. Shiga Like Toxin-1 Subunit B has nontoxic action, it is the functional region which binds to the receptor. The Shiga Like Toxin-1 Subunit B can be useful in vaccine study, antibody test and other functional research.
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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.
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Purification Method
Purified by affinity chromatographic technique.
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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Name :
Soybean P34 GSTDescription:
Soybean P34 Protein Recombinant, GST Tag
Product # :
ALR-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.Coli derived GST Tag recombinant protein, 36kDa, contains Soybean P34 Protein epitopes 214-261, 351-379 amino acids.
Source
Escherichia Coli.
Formulation
50mM Tris-HCl, pH 8.0, 60mM NaCl, 10mM glutathione and 50% glycerol.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
The P34 protein is the main allergen for soybean sensitive humans. Soybean protein P34, a thiol protease belonging to the papain family, is a monomeric allergen having an N-terminal amino acid sequence and amino acid composition identical to that of the seed 34kDa protein. It is an insoluble glycoprotein having a pI of 4.5 and a calculated mass of 28.643 Dalton, representing 2–3% of total soybean protein. Upon glycosylation, the mass will be somewhat larger, resulting in a ~32kDa band in non-reduced SDS PAGE gels. It exhibits no enzymatic function due to an absence of the catalytic cysteine. P34 is stored in storage vacuoles of soybean cotyledons.
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Stability
Soybean P34 His although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Purification Method
Purified by proprietary chromatographic technique
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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Name :
FGB HumanDescription:
Fibrinogen Beta Chain Human Recombinant
Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.
Product # :
PRO-2210Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FGB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 351 amino acids (164-491a.a) and having a molecular mass of 40kDa. FGB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FGB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Fibrinogen Beta Chain 9 (FGB) is the beta component of fibrinogen, a blood-borne glycoprotein composed of 3 pairs of nonidentical polypeptide chains. When vascular injury accrues, fibrinogen is cleaved by thrombin to form fibrin which is found in abundance in blood clots.
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Synonyms
Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDNENVVN EYSSELEKHQ LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM SMKIRPFFPQ Q.
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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Name :
BMP 4 HumanDescription:
Bone Morphogenetic Protein-4 Human Recombinant
BMP4, ZYME, BMP2B, BMP2B1.
Product # :
CYT-361Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.
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Synonyms
BMP4, ZYME, BMP2B, BMP2B1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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.
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Solubility
It is recommended to reconstitute the lyophilized Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
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Background
What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant
As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.
Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.
Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!
How Does Bone Morphogenetic Protein-4 (BMP-4) Work?
Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.
The Role of BMP-4
This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.
However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:
- Embryonic development
- Wound healing
- Bone remodeling
- Immune response modulation
- Tissue repair
- Cardiac development and function
What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?
To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.
As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.
More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:
- Cancer therapy
- Development of engineered tissues and organs
- Bone regeneration for the treatment of osteoporosis and nonunion fractures
- Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
- Promotion of tissue repair and regeneration
Final Thoughts BMP-4
Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.
However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.
What is the molecular weight/Mw of BMP4 Protein?
BMP4 Protein has a total Mw of 13kDa.
What is the source or expression system of BMP4 Protein?
Escherichia Coli.
What is the Purity of BMP4 Protein?
BMP4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP4 Protein?
The biological functionality of BMP4 Protein will be determined in the future.
What is the amino acid sequence of BMP4 Protein?
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
What applications can BMP4 Protein be used in?
BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP4 Protein?
The endotoxin level is minimal, BMP4 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.
- View Data Sheet
Name :
GHRP1Description:
Growth Hormone Releasing Peptide-1
GHRP-1, GHRP1.
Product # :
HOR-021Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- More Info
Description
Growth Hormone Releasing Peptide-1 Synthetic is a single, non-glycosylated polypeptide chain containing 5 amino acids, having a molecular mass of 955.11 Dalton and a Molecular formula of C51H62N12O7.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Introduction
GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH effect on pituitary somatotrophs to stimulate GH release. The GHRP1 is one of several synthetic met-enkephalin analogs that owns unnatural D-amino acids. They were developed for their growth hormone (GH) releasing activity and called GH secretatogues. They lack opioid activity but are potent stimulators of GH release. These secretatogues are distinct from the growth hormone releasing hormone (GHRH or GHRF) as they share no sequence relation and derive their function through action at a completely different receptor, the ghrelin receptor.
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Synonyms
GHRP-1, GHRP1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth Hormone Releasing Peptide-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP1 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.
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Solubility
It is recommended to reconstitute the lyophilized GHRP1 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Ala-His-(D-β-Nal)-Ala-Trp-(D-Phe)-Lys-NH2.
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.
- View Data Sheet
Name :
CRYBA4 HumanDescription:
Crystallin Beta A4 Human Recombinant
Beta-crystallin A4, Beta-A4 crystallin, CRYBA4, MCOPCT4.
Product # :
HSP-048Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRYBA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-196 a.a.) and having a molecular mass of 24.5kDa.CRYBA4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYBA4 protein (1mg/ml) 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Beta-crystallin A4 (CRYBA4) is a member of the beta/gamma-crystallin family which are the dominant structural components of the vertebrate eye lens. Beta-crystallins construct aggregates of various sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. The CRYBA4 gene being a beta acidic group member is part of a gene cluster with beta-B1, beta-B2, and beta-B3.
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Synonyms
Beta-crystallin A4, Beta-A4 crystallin, CRYBA4, MCOPCT4.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTLQCTKSAG PWKMVVWDED GFQGRRHEFT AECPSVLELG FETVRSLKVL SGAWVGFEHA GFQGQQYILE RGEYPSWDAW GGNTAYPAER LTSFRPAACA NHRDSRLTIF EQENFLGKKG ELSDDYPSLQ AMGWEGNEVG SFHVHSGAWV CSQFPGYRGF QYVLECDHHS GDYKHFREWG SHAPTFQVQS IRRIQQ.
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.
- View Data Sheet
Name :
CoV-2 N-MosaicDescription:
Coronavirus 2019 Nucleocapsid Mosaic Recombinant
Product # :
SARS-015Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
The E.Coli derived recombinant protein contains the Coronavirus 2019 full length nuclepocapsid Mosaic immunodominant regions [ full length N-antigen ], fused to 6xHis tag at C-terminal.
Source
Escherichia Coli.
Formulation
CoV 2019 Nucleocapsid-Mosaic Protein solution is supplied in 1x PBS.
Purity
CoV 2019 Nucleocapsid-Mosaic Protein ein is >90% pure as determined SDS-PAGE.
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
CoV 2019 Nucleocapsid-Mosaic Protein is shipped on ice packs. Upon arrival, Store at -20°C.
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Specificity
Reactivity with SARS infected individuals not tested.
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.
- View Data Sheet
Name :
Follistatin HumanDescription:
Follistatin Human Recombinant
FST, FS
Product # :
CYT-232Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
More Info
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
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Synonyms
FST, FS
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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.
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Solubility
It is recommended to reconstitute the lyophilized Follistatin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
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Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.
What is the source or expression system of FOLLISTATIN HUMAN Protein?
Escherichia Coli.
What is the Purity of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
What applications can FOLLISTATIN HUMAN Protein be used in?
FOLLISTATIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN Protein?
The endotoxin level is minimal, FOLLISTATIN 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.
- View Data Sheet
Name :
Cyclophilin B HumanDescription:
Cyclophilin-B Human Recombinant
Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.
Product # :
ENZ-313Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Cyclophilin-B Human Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 192 amino acids (26-216) and having a molecular mass of 21.2 kDa. PPIB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 20mM Tris-HCl 8.0, 20mM NaCl, 0.5mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.
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Synonyms
Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MLLPGPSAAD EKKKGPKVTV KVYFDLRIGD EDVGRVIFGL FGKTVPKTVD NFVALATGEKGFGYKNSKFH RVIKDFMIQG GDFTRGDGTG GKSIYGERFP DENFKLKHYG PGWVSMANAGKDTNGSQFFI TTVKTAWLDG KHVVFGKVLE GMEVVRKVES TKTDSRDKPL KDVIIADCGK IEVEKPFAIA KE.
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.