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Search results

1000 results found for “Calponin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    TMEFF1 Human

    Description:

    TMEFF1 Human Recombinant

    C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.

    Product # :

    PRO-1429

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    Description

    TMEFF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 314 amino acids (40-330) and having a molecular mass of 33.9kDa. TMEFF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TMEFF1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TMEFF1 is a type I transmembrane glycoprotein which includes 2 follistatin modules and an EGF domain in its extracellular domain, a transmembrane domain and a short cytoplasmic tail. The extracellular domain of TMEFF1 can be released as a soluble protein. TMEFF1 is primarily expressed in brain, but is downregulated in brain neoplasms. TMEFF1 selectively regulates nodal but not activin signaling through direct binding to the nodal co-receptor, Cripto. TMEFF inhibits NODAL and BMP signaling through neural patterning and also a possible tumor suppressor in brain cancers.

    • Synonyms

      C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.

    • 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 MGSSNQPPGG GGGSGGDCPG GKGKSINCSE LNVRESDVRV CDESSCKYGG VCKEDGDGLK CACQFQCHTN YIPVCGSNGD TYQNECFLRR AACKHQKEIT VIARGPCYSD NGSGSGEGEE EGSGAEVHRK HSKCGPCKYK AECDEDAENV GCVCNIDCSG YSFNPVCASD GSSYNNPCFV REASCIKQEQ IDIRHLGHCT DTDDTSLLGK KDDGLQYRPD VKDASDQRED VYIGNHMPCP ENLNGYCIHG KCEFIYSTQK ASCRCESGYT GQHCEKTDFS ILYVVPSRQK LTHV.

    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.

    Tmeff1 Human
  • View Data Sheet

    Name :

    TRAPPC3 Human

    Description:

    Trafficking Protein Particle Complex 3 Human Recombinant

    Trafficking protein particle complex subunit 3, BET3, BET3 homolog, 1110058K12Rik.

    Product # :

    PRO-1056

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    Description

    TRAPPC3 Human Recombinant produced in E. coli is a single polypeptide chain containing 200 amino acids (1-180) and having a molecular mass of 22.4kDa.TRAPPC3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TRAPPC3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TRAPPC3 is a part of the TRAPP complex that takes part in connection of transport vesicles to the cis-Golgi membrane. Additionally, TRAPPC3 is involved in vesicular transport from endoplasmic reticulum to Golgi.

    • Synonyms

      Trafficking protein particle complex subunit 3, BET3, BET3 homolog, 1110058K12Rik.

    • 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 MSRQANRGTE SKKMSSELFT LTYGALVTQL CKDYENDEDV NKQLDKMGFN IGVRLIEDFL ARSNVGRCHD FRETADVIAK VAFKMYLGIT PSITNWSPAG DEFSLILENN PLVDFVELPD NHSSLIYSNL LCGVLRGALE MVQMAVEAKF VQDTLKGDGV TEIRMRFIRR IEDNLPAGEE

    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.

    Trappc3 Human
  • View Data Sheet

    Name :

    Glucagon Human, His

    Description:

    Glucagon Human Recombinant, His Tag

    Glucagon, GCG, GLP1, GLP2, GRPP.

    Product # :

    HOR-301

    Price :

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    Description

    Glucagon Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (90-180 a.a.) and having a molecular mass of 12.8kDa.Glucagon is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Glucagon protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
      Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract.

    • Synonyms

      Glucagon, GCG, GLP1, GLP2, GRPP.

    • 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 MKRHDEFERH AEGTFTSDVS SYLEGQAAKE FIAWLVKGRG RRDFPEEVAI VEELGRRHAD GSFSDEMNTI LDNLAARDFI NWLIQTKITD RK.

    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.

    Glucagon Human His
  • View Data Sheet

    Name :

    CKBB Human, Active

    Description:

    Creatine Kinase Brain Human Recombinant, Active

    Creatine kinase B-type, EC 2.7.3.2, Creatine kinase B chain, B-CK, CKB, CKBB, CKBBI.

    Product # :

    CKI-268

    Price :

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    Description

    CKBB Human Recombinant produced in Pichia Pastoris is a dimeric glycosylated full length polypeptide chain comprised of 2 identical B subunits and having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and having a Mw of 47kDa The CKBB is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    CKBB Human contains 10Mm Bis-Tris-HCl pH-6.0, 50% glycerol, 0.5mM EDTA and 0.5mM DTT.

    Purity

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

    Biological Activity

    The biological activity of CKBB was measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 854 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 1,171ng/ml.

    More Info

    • Introduction

      Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.

    • Synonyms

      Creatine kinase B-type, EC 2.7.3.2, Creatine kinase B chain, B-CK, CKB, CKBB, CKBBI.

    • Physical Appearance

      Sterile Filtered colourless liquid formulation.

    • Stability

      CKBB should be stored below -18°C. Please prevent 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.

    Ckbb Human
  • View Data Sheet

    Name :

    CXCL3 Mouse, His

    Description:

    GRO-Gamma Mouse Recombinant (CXCL3), His Tag

    C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    Product # :

    CHM-283

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    Description

    GRO-g Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (28-100 a.a.) and having a molecular mass of 10.6kDa.CXCL3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GRO-gamma protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.15M NaCl and 5mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.

    • Synonyms

      C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    • 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 MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

    • Background

      What is the molecular weight/Mw of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein has a total Mw of 10.6kDa.

      What is the source or expression system of CXCL3 MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL3 MOUSE, HIS Protein?
      The biological functionality of CXCL3 MOUSE, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL3 MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

      What applications can CXCL3 MOUSE, HIS Protein be used in?
      CXCL3 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL3 MOUSE, HIS Protein?
      The endotoxin level is minimal, CXCL3 MOUSE, HIS Protein was purified using conventional chromatography techniques.


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

    Gro G Mouse His
  • View Data Sheet

    Name :

    RAPSN Mouse

    Description:

    Receptor-Associated Protein Of The Synapse Mouse Recombinant

    Receptor-Associated Protein Of The Synapse, 43 KDa Postsynaptic Protein, Acetylcholine Receptor-Associated 43 KDa Protein, RNF205, RING Finger Protein 205, rapsyn, Receptor-Associated Protein Of The Synapse, 43Kd, 43 KDa Receptor-Associated Protein Of The Synapse, RAPSYN, RAPsyn, CMS1D, CMS1E.

    Product # :

    PRO-1751

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    Description

    RAPSN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 435 amino acids (1-412aa) and having a molecular mass of 48.8kDa.RAPSN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RAPSN protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      43 kDa receptor-associated protein of the synapse (RAPSN), is expressed in the postsynaptic membrane of skeletal muscle. RAPSN is essential for the clustering of nicotinic acetylcholine receptors (nAChR). In addition RAPSN self-associates via at least two of its seven tetra-tricopeptide repeats (TPRs). RAPSN interacts with the large intracellular domain of the nAChR a subunit all the way through the hydrophobic surface of the coiled-coil domain. RAPSN modifies trafficking of AChR within the cell. Overexpression inhibits agrin-induced AChR clustering pathway. RAPSN also plays a role in postsynaptic congenital myasthenic syndromes.

    • Synonyms

      Receptor-Associated Protein Of The Synapse, 43 KDa Postsynaptic Protein, Acetylcholine Receptor-Associated 43 KDa Protein, RNF205, RING Finger Protein 205, rapsyn, Receptor-Associated Protein Of The Synapse, 43Kd, 43 KDa Receptor-Associated Protein Of The Synapse, RAPSYN, RAPsyn, CMS1D, CMS1E.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMGQDQTK QQIEKGLQLY QSNQTEKALQ VWMKVLEKGS DLVGRFRVLG CLVTAHSEMG RYKEMLKFAV VQIDTARGLE DADFLLESYL NLARSNEKLC EFHKTISYCK TCLGLPGTRA GAQLGGQVSL SMGNAFLGLS LFQKALESFE KALRYAHNND DTMLECRVCC SLGSFYAQVK DYEKALFFPC KAAELVNDYG KGWSLKYRAM SQYHMAVAYR LLGHLGSAME CCEESMKIAL QHGDRPLQAL CLLCFADIHR SRGDLETAFP RYDSAMSIMT EIGNRLGQVH VLLGVAKCWM ARKVQDKALD AIEKAQDLAE EVGNKLSQLK LHCLSESIYR SKGLQRELRT HVVRFHECVE ETELYCGLCG ESIGERNSRL QALPCSHIFH LRCLQNNGTR SCPNCRRSSM KPGFV

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    Rapsn Mouse
  • View Data Sheet

    Name :

    MESDC2 Mouse

    Description:

    Mesoderm Development Candidate 2 Mouse Recombinant

    LDLR chaperone MESD, Mesoderm development candidate 2, Mesoderm development protein, Mesdc2, Mesd.

    Product # :

    PRO-2260

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    Description

    MESDC2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (30-224 a.a) and having a molecular mass of 24.4kDa. MESDC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MESDC2 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mesoderm development candidate 2 (MESDC2) is required for formation of the primitive streak and mesoderm during embryogenesis. MESDC2 binds to the Wnt co-receptors LRP5 and LRP6 in the endoplasmic reticulum and is required for their proper folding and cell surface expression.

    • Synonyms

      LDLR chaperone MESD, Mesoderm development candidate 2, Mesoderm development protein, Mesdc2, Mesd.

    • 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 MGSADTPGEA TPPPRKKKDI RDYNDADMAR LLEQWEKDDD IEEGDLPEHK RPSAPIDFSK LDPGKPESIL KMTKKGKTLM MFVTVSGNPT EKETEEITSL WQGSLFNANY DVQRFIVGSD RAIFMLRDGS YAWEIKDFLV SQDRCAEVTL EGQMYPGKGG GSKEKNKTKP EKAKKKEGDP KPRASKEDNR AGSRREDL.

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    Mesdc2 Mouse
  • View Data Sheet

    Name :

    SELANK

    Description:

    SELANK

    Product # :

    HOR-035

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    Description

    SELANK Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 751.89 Dalton and a Molecular formula of C33H57N11O9.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SELANK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELANK 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 SELANK in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Thr-Lys-Pro-Arg-Pro-Gly-Pro-OH.

    • Background

      Selank, also known as TP-7, is a synthetic peptide that has garnered significant attention in the scientific community due to its potential anxiolytic, neuroprotective, and nootropic effects. This heptapeptide, derived from the naturally occurring human tetrapeptide Tuftsin, has been shown to possess a wide range of biological activities, including enhancing memory, reducing anxiety, and potentially mitigating the effects of neurodegenerative diseases.

      Selank's primary mechanism of action involves its interaction with the GABAergic system, the body's main inhibitory neurotransmitter system. By modulating the activity of GABA receptors, Selank can exert a calming effect on the brain, reducing anxiety and enhancing cognitive function. Studies by Semenova et al. (2014) have demonstrated that Selank can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.

      In addition to its anxiolytic and nootropic effects, Selank has been shown to possess neuroprotective properties. Research by Ershov et al. (2016) found that Selank could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.

      Given its anxiolytic, nootropic, and neuroprotective effects, Selank has been proposed as a potential therapeutic agent for a variety of conditions, including anxiety disorders, cognitive disorders, and neurodegenerative diseases. For instance, a study by Medvedev et al. (2017) found that Selank could improve symptoms in patients with generalized anxiety disorder, indicating its potential as a therapeutic agent in the treatment of anxiety disorders.

      While research on Selank is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of Selank in humans. However, the existing body of research suggests that Selank could be a promising tool in the treatment of anxiety disorders, cognitive disorders, and neurodegenerative diseases.

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    Selank
  • View Data Sheet

    Name :

    HCV Core Genotype-3/10

    Description:

    Hepatitis C Virus Core Genotype-3/10 Recombinant

    Product # :

    HCV-201

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    Description

    The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119.

    Source

    Escherichia Coli.

    Formulation

    50mM Tris-HCl, pH-8, 60mM NaCl, 10mM glutathione, 0.25% sarkosil & 50% glycerol.

    Purity

    HCV Core Genotype-3/10 protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
      HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

    • Stability

      HCV Core Genotype-3/10 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HCV Core Genotype-3/10 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HCV-infected individuals.

    • Purification Method

      HCV Core Genotype-3/10 protein was 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.

    Hcv Core Genotype 3 10
  • View Data Sheet

    Name :

    Protein-A/G/L-Cys

    Description:

    Protein A/G/L-Cys Recombinant

    Product # :

    PRO-1934

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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 806 amino acids in total and having a molecular mass of 89.3kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein- A/G/L was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.

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    Protein A G L Cys
  • View Data Sheet

    Name :

    HPSE WB

    Description:

    Recombinant Human Heparanase-1 WB Control

    Product # :

    ENZ-261

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    Description

    Recombinant Heparanase protein HPA1 is produced in CHO cells.The protein is purified by several orthogonal chromatography steps.

    Formulation

    Concentration: 1μg /ml
    Content: 100 ng
    Buffer: LDS-PAGE buffer
    [140 mM Tris buffer pH 8.5, 10% Glycerol, 2% LDS, 0.015% EDTA, 1.88% (v/v) of 1% Serva Blue G250 and 0.625% (v/v) of 1% Phenol red].

    More Info

    • Introduction

      Heparanase is an endo β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).

    • Applications

      Positive control for western blot analysis.

    • Preparation protocol

      Use 20 μl of recombinant human heparanase 1 (HPA1) per lane, as a control for using monoclonal anti HPA 1 clone HP3/17 antibodies (Cat. No.: Ins-AB-04001) or polyclonal rabbit anti HPA1 antibody (Cat. No.: Ins-AB-04002).

    • Data Sheet

      To view the FULL VERSION data sheet click Heparanase-1 WB Protein:

    • Storage Procedures

      Store at –20ºC, avoid repeated freeze-thaw cycles.

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    Heparanase Human
  • View Data Sheet

    Name :

    CDCP1 Human

    Description:

    CUB Domain Containing Protein 1 Human Recombinant

    CUB Domain Containing Protein 1, Subtractive Immunization M Plus HEp3-Associated 135 KDa Protein, Transmembrane And Associated With Src Kinases, Membrane Glycoprotein Gp140, SIMA135, TRASK, CD318 Antigen, CD318, CUB domain-containing protein 1, Membrane glycoprotein gp140, Subtractive immunization M plus HEp3-associated 135 kDa protein, Transmembrane and associated with src kinases.

    Product # :

    PRO-2264

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    Description

    CDCP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 646 amino acids (30-667a.a.) and having a molecular mass of 72.8kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). CDCP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CDCP1 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

    • Introduction

      CUB Domain Containing Protein 1, also known as CDCP1 is a transmembrane protein which contains three extracellular CUB domains. CDCP1 is implicated in cell adhesion and cell matrix association. In addition, CDCP1 takes part in the regulation of anchorage versus migration or proliferation versus differentiation through its phosphorylation. CDCP1 is also a novel marker for leukemia diagnosis as well as for immature hematopoietic stem cell subsets. Furthermore, the extracellular region of human CDCP1 shares amino acid identity sequence with the mouse CDCP1.

    • Synonyms

      CUB Domain Containing Protein 1, Subtractive Immunization M Plus HEp3-Associated 135 KDa Protein, Transmembrane And Associated With Src Kinases, Membrane Glycoprotein Gp140, SIMA135, TRASK, CD318 Antigen, CD318, CUB domain-containing protein 1, Membrane glycoprotein gp140, Subtractive immunization M plus HEp3-associated 135 kDa protein, Transmembrane and associated with src kinases.

    • 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

      FEIALPRESN ITVLIKLGTP TLLAKPCYIV ISKRHITMLS IKSGERIVFT FSCQSPENHF VIEIQKNIDC MSGPCPFGEV QLQPSTSLLP TLNRTFIWDV KAHKSIGLEL QFSIPRLRQI GPGESCPDGV THSISGRIDA TVVRIGTFCS NGTVSRIKMQ EGVKMALHLP WFHPRNVSGF SIANRSSIKR LCIIESVFEG EGSATLMSAN YPEGFPEDEL MTWQFVVPAH LRASVSFLNF NLSNCERKEE RVEYYIPGST TNPEVFKLED KQPGNMAGNF NLSLQGCDQD AQSPGILRLQ FQVLVQHPQN ESNKIYVVDL SNERAMSLTI EPRPVKQSRK FVPGCFVCLE SRTCSSNLTL TSGSKHKISF LCDDLTRLWM NVEKTISCTD HRYCQRKSYS LQVPSDILHL PVELHDFSWK LLVPKDRLSL VLVPAQKLQQ HTHEKPCNTS FSYLVASAIP SQDLYFGSFC PGGSIKQIQV KQNISVTLRT FAPSFQQEAS RQGLTVSFIP YFKEEGVFTV TPDTKSKVYL RTPNWDRGLP SLTSVSWNIS VPRDQVACLT FFKERSGVVC QTGRAFMIIQ EQRTRAEEIF SLDEDVLPKP SFHHHSFWVN ISNCSPTSGK QLDLLFSVTL TPRTVDLTLE HHHHHH.

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    Cdcp1 Human
  • View Data Sheet

    Name :

    Leptin Protein

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

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    Description

    Leptin Human 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 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • 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.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin in sterile water or 0.4% NaHCO3 pH-8-9, 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 Ala-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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).

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    Leptin Human
  • View Data Sheet

    Name :

    Cadherin-E Human

    Description:

    Cadherin-E Human Recombinant

    Epithelial cadherin, E-cadherin, Uvomorulin, Cadherin-1, CAM 120/80, CD324 antigen, CDH1, CDHE, UVO, ECAD, LCAM, Arc-1, CD324, Cadherin-E.

    Product # :

    PRO-461

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    Description

    Cadherin-E Human Recombinant (aa 600-707) expressed in E.coli, shows a 38 kDa band on SDS-PAGE.The Cadherin-E is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cadherin-E protein (100µg/1ml) in 50mM Tris-HCl, pH7.5 and 10mM L-glutathione (reduced).

    More Info

    • Introduction

      E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. It plays an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Numerous studies have demonstrated that reduction and/or loss of Ecadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis.

    • Synonyms

      Epithelial cadherin, E-cadherin, Uvomorulin, Cadherin-1, CAM 120/80, CD324 antigen, CDH1, CDHE, UVO, ECAD, LCAM, Arc-1, CD324, Cadherin-E.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      iffcernpkpq viniidadlp pntspftael thgasanwti qyndptqesi ilkpkmalev gdykinlklm dnqnkdqvtt levsvcdceg aagvcrkaqp veaglqi.

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    E Cadherin Human
  • View Data Sheet

    Name :

    IL 4 Mouse

    Description:

    Interleukin-4 Mouse Recombinant

    BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

    Product # :

    CYT-282

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    Description

    Interleukin-4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13500 Dalton. The IL-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm 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 as determined by the dose-dependant induction of HT-2 cell proliferation is less than 2 ng/ml corresponding to a Specific Activity of 500,000IU/mg.

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    • Introduction

      Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.

    • Synonyms

      BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 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 Interleukin 4 in sterile 10mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHIHGCDKNH LREIIGILNE VTGEGTPCTE MDVPNVLTAT KNTTESELVC RASKVLRIFY LKHGKTPCLK KNSSVLMELQ RLFRAFRCLD SSISCTMNES KSTSLKDFLE SLKSIMQMDY 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.

    Il 4 Mouse
  • View Data Sheet

    Name :

    Leptin Super Antagonist Human

    Description:

    Leptin Super Antagonist Human Recombinant

    Product # :

    CYT-1238

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    Description

    Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Super Leptin Antagonist 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.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Background

      Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

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    Leptin Antagonist Super Human
  • View Data Sheet

    Name :

    CRMP1 Mouse

    Description:

    Collapsin Response Mediator Protein-1 Mouse Recombinant

    Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.

    Product # :

    PRO-2521

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    Description

    CRMP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (1-572 a.a) and having a molecular mass of 64.8kDa.CRMP1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CRMP1 protein solution (0.25mg/ml) contains 40% glycerol, 20mM Tris-HCl (pH 8.5), 0.2M NaCl & 0.1mM PMSF.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation as well as axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The X-ray crystal structure of murine CRMP1 was determined at 2.1 resolution and demonstrates that CRMP1 is a bilobed ‘lung-shaped’ protein forming a tetrameric assembly.

    • Synonyms

      Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.

    • 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 MGSEFMSHQG KKSIPHITSD RLLIRGGRII NDDQSFYADV YLEDGLIKQI GENLIVPGGV KTIEANGRMV IPGGIDVNTY LQKPSQGMTS ADDFFQGTKA ALAGGTTMII DHVVPEPGSS LLTSFEKWHE AADTKSCCDY SLHVDITSWY DGVREELEVL VQDKGVNSFQ VYMAYKDLYQ MSDSQLYEAF TFLKGLGAVI LVHAENGDLI AQEQKRILEM GITGPEGHAL SRPEELEAEA VFRAIAIAGR INCPVYITKV MSKSAADIIA LARKKGPLVF GEPIAASLGT DGTHYWSKNW AKAAAFVTSP PLSPDPTTPD YLTSLLACGD LQVTGSGHCP YSTAQKAVGK DNFTLIPEGV NGIEERMTVV WDKAVATGKM DENQFVAVTS TNAAKIFNLY PRKGRIAVGS DADVVIWDPD KMKTITAKSH KSTVEYNIFE GMECHGSPLV VISQGKIVFE DGNISVSKGM GRFIPRKPFP EHLYQRVRIR SKVFGLHSVS RGMYDGPVYE VPATPKHAAP APSAKSSPSK HQPPPIRNLH QSNFSLSGAQ IDDNNPRRTG HRIVAPPGGR SNITSLG.

    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.

    CRMP1 Mouse
  • View Data Sheet

    Name :

    MFGE8 Mouse

    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.

    More Info

    • 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.

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    Mfge8 Mouse
  • View Data Sheet

    Name :

    CTSZ Mouse, Active

    Description:

    Cathepsin-Z, Active Mouse Recombinant

    Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    Product # :

    ENZ-1108

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    Description

    CTSZ Mouse Recombinant produced in Baculovirus is a single, glycosylated, polypeptide chain containing 292 amino acids (23-306 aa) and having a molecular mass of 32.8kDa.CTSZ is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3,000 pmol/min/ug. One unit will convert 1 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25°C.

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    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    • 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

      ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT
      RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV
      WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE
      KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV
      RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH HH

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    Cathepsin Z Mouse
  • View Data Sheet

    Name :

    ARPC2 Human

    Description:

    Actin Related Protein 2/3 Complex, Subunit 2 Human Recombinant

    ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.

    Product # :

    PRO-1418

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    Description

    ARPC2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300a.a) and having a molecular mass of 36.7kDa. ARPC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ARPC2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Actin-related protein 2/3 complex subunit 2 (ARPC2), is a part of the Rho family of small GTPases and one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. Nevertheless, the exact role of the protein (the p34 subunit) has yet to be determined.

    • Synonyms

      ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.

    • 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 MGSMILLEVN NRIIEETLAL KFENAAAGNK PEAVEVTFAD FDGVLYHISN PNGDKTKVMV SISLKFYKEL QAHGADELLK RVYGSFLVNP ESGYNVSLLY DLENLPASKD SIVHQAGMLK RNCFASVFEK YFQFQEEGKE GENRAVIHYR DDETMYVESK KDRVTVVFST VFKDDDDVVI GKVFMQEFKE GRRASHTAPQ VLFSHREPPL ELKDTDAAVG DNIGYITFVL FPRHTNASAR DNTINLIHTF RDYLHYHIKC SKAYIHTRMR AKTSDFLKVL NRARPDAEKK EMKTITGKTF SSR.

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    Arpc2 Human
  • View Data Sheet

    Name :

    SNCG Mouse

    Description:

    Gamma-Synuclein Mouse Recombinant

    Gamma-synuclein, Persyn.

    Product # :

    PRO-2490

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    Description

    SNCG Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 146 amino acids (1-123 a.a) and having a molecular mass of 15.5kDa.SNCG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNCG protein solution (1mg/ml) containing 20mM Tris-HCl(pH8.0) and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      g-synuclein(Originally known as a breast cancer specific gene product, BCSG1) is an acidic neuronal protein of 127 amino acids. Gamma-Synuclein is a member of the Synuclein protein family, which is believed to be involved in the pathogenesis of neurodegenerative diseases. High levels of Gamma-Synuclein have been found in advanced breast carcinomas suggesting a correlation between overexpression of SNCG and breast tumor development. Synuclein-Gamma is found mostly in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. SNCG is also identified in the brain, ovarian tumors, and in the olfactory epithelium. SNCG expression in breast tumors is a marker for tumor progression. A modification in the expression of gamma-synuclein has been detected in the retina of Alzheimer's patients.

    • Synonyms

      Gamma-synuclein, Persyn.

    • 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 MGSMDVFKKG FSIAKEGVVG AVEKTKQGVT EAAEKTKEGV MYVGTKTKEN VVQSVTSVAE KTKEQANAVS AVVSSVNTV ANKTVEEAEN IVVTTGVVRK EDLEPPAQDQ EAKEQEENEE AKSGED.

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    Sncg Mouse
  • View Data Sheet

    Name :

    USP46 Human

    Description:

    Ubiquitin Specific Peptidase 46 Human Recombinant

    Ubiquitin carboxyl-terminal hydrolase 46, Deubiquitinating enzyme 46, Ubiquitin thioesterase 46, Ubiquitin-specific-processing protease 46, USP46.

    Product # :

    PRO-1866

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    Description

    USP46 Human Recombinant produced in E. coli is. a single polypeptide chain containing 389 amino acids (1-366) and having a molecular mass of 44.8kDa. USP46 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The USP46 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      USP46 is a part of a large family of cysteine proteases that function as deubiquitinating enzymes which interacts with WDR48 to have a high activity. USP46 operates by mediating the deubiquitination of GAD1/GAD67.

    • Synonyms

      Ubiquitin carboxyl-terminal hydrolase 46, Deubiquitinating enzyme 46, Ubiquitin thioesterase 46, Ubiquitin-specific-processing protease 46, USP46.

    • 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 MGSMTVRNIA SICNMGTNAS ALEKDIGPEQ FPINEHYFGL VNFGNTCYCN SVLQALYFCR PFRENVLAYK AQQKKKENLL TCLADLFHSI ATQKKKVGVI PPKKFISRLR KENDLFDNYM QQDAHEFLNY LLNTIADILQ EEKKQEKQNG KLKNGNMNEP AENNKPELTW VHEIFQGTLT NETRCLNCET VSSKDEDFLD LSVDVEQNTS ITHCLRDFSN TETLCSEQKY YCETCCSKQE AQKRMRVKKL PMILALHLKR FKYMEQLHRY TKLSYRVVFP LELRLFNTSS DAVNLDRMYD LVAVVVHCGS GPNRGHYITI VKSHGFWLLF DDDIVEKIDA QAIEEFYGLT SDISKNSESG YILFYQSRE.

    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.

    Usp46 Human
  • View Data Sheet

    Name :

    HAPLN1 Human, HEK

    Description:

    Hyaluronan And Proteoglycan Link Protein 1 Human Recombinant, HEK

    Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.

    Product # :

    PRO-2776

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    Description

    HAPLN1 Human Recombinant produced in HEK293 Cells.is a single, glycosylated polypeptide chain containing 345 amino acids (16-354 a.a.) and having a molecular mass of 39.3kDa. HAPLN1 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    HAPLN1 protein solution (0.25mg/ml) containing 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤ 1 ug/ml and is measured by its binding ability in a functional ELISA with Hyaluronic acid.

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    • Synonyms

      Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.

    • 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

      DHLSDNYTLD HDRAIHIQAE NGPHLLVEAE QAKVFSHRGG NVTLPCKFYR DPTAFGSGIH KIRIKWTKLT SDYLKEVDVF VSMGYHKKTY GGYQGRVFLK GGSDSDASLV ITDLTLEDYG RYKCEVIEGL EDDTVVVALD LQGVVFPYFP RLGRYNLNFH EAQQACLDQD AVIASFDQLY DAWRGGLDWC NAGWLSDGSV QYPITKPREP CGGQNTVPGV RNYGFWDKDK SRYDVFCFTS NFNGRFYYLI HPTKLTYDEA VQACLNDGAQ IAKVGQIFAA WKILGYDRCD AGWLADGSVR YPISRPRRRC SPTEAAVRFV GFPDKKHKLY GVYCFRAYNH HHHHH.

    • Background

      Bibliography:

      Armingol, E., Officer, A., Harismendy, O., & Lewis, N. E. (2020). Deciphering cell-cell interactions and communication from gene expression. Nature Reviews Genetics, 21(2), 71-88.

      Bonnans, C., Chou, J., & Werb, Z. (2014). Remodelling the extracellular matrix in development and disease. Nature Reviews Molecular Cell Biology, 15(12), 786-801.

      Bönnemann, C. G. (2011). The collagen VI-related myopathies: muscle meets its matrix. Nature Reviews Neurology, 7(7), 379-390.

      Choi, H., Lee, R. H., Bazhanov, N., Oh, J. Y., & Prockop, D. J. (2011). Anti-inflammatory protein TSG-6 secreted by activated MSCs attenuates zymosan-induced mouse peritonitis by decreasing TLR2/NF-κB signaling in resident macrophages. Blood, 118(2), 330-338.

      Lesley, J., Hyman, R., & Kincade, P. W. (1993). CD44 and its interaction with extracellularmatrix. Advances in Immunology, 54, 271-335.

      Sherman, L. S., Rizvi, T. A., Karyala, S., & Ratner, N. (2000). CD44 enhances neuregulin signaling by Schwann cells. The Journal of Cell Biology, 150(5), 1071-1084.

      Toole, B. P. (2004). Hyaluronan: from extracellular glue to pericellular cue. Nature Reviews Cancer, 4(7), 528-539.

      Yamada, Y., Itano, N., Narimatsu, H., Kudo, T., Morozumi, K., Hirohashi, S., ... & Kimata, K. (2004). Elevated transcript level of hyaluronan synthase1 gene correlates with poor prognosis of human colon cancer. Clinical & Experimental Metastasis, 21(1), 57-63.

    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.

    Hapln1 Human Hek
  • View Data Sheet

    Name :

    VEGF (121 a.a.) Human

    Description:

    Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant

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

    Product # :

    CYT-343

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    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

    • 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.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • 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.

    • 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.

    Vegf121 Human
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