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Search results

1000 results found for “uroplakin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    UBE2V2 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2 Variant 2 Human Recombinant

    DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.

    Product # :

    ENZ-550

    Price :

    Quantity :

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    • description
    • source
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    • More Info

    Description

    UBE2V2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145 a.a.) and having a molecular mass of 18.5 kDa. The UBE2V2 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2V2 Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2V2 comprises a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes however require the conserved cysteine residue that is vital for the catalytic activity of E2s. UBE2V2 shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product. UBE2V2 participates in the differentiation of monocytes and enterocytes.

    • Synonyms

      DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.

    • 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 MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ ELRRLMMSKE NMKLPQPPEG QTYNN.

    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.

    Ube2V2 Human
  • View Data Sheet

    Name :

    R-Spondin-1 Human

    Description:

    R-Spondin-1 Human Recombinant

    R-spondin-1, Cristin-3, mCristin-3, Roof plate-specific spondin-1, Rspo1, RSPO, R-spondin 1, R-spondin, Rspondin, CRISTIN3.

    Product # :

    PRO-2593

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    • More Info

    Description

    R-Spondin-1 Human Recombinant produced in CHO cells is a glycosylated monomer chain containing 243 amino acids and having a total molecular mass of 25.6kDa. RSPO1 is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    The protein was lyophilized from a sterile (0.2µm) filtered solution containing PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as calculated by the Luciferase induction in HEK-293 STF cells in the presence of Murine Wnt-3a is 47.99ng/ml corresponding to a specific activity of 2.1 x 10^4 units/mg.

    More Info

    • Introduction

      R-Spondin-1 (Rspo1) is a part of the Rspondin family. Rspo1 plays a role as an activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Rspo1 induces the onset of crypt cell proliferation and increases intestinal epithelial healing effect. Rspo1 is negatively regulating the TGF-beta pathway.

    • Synonyms

      R-spondin-1, Cristin-3, mCristin-3, Roof plate-specific spondin-1, Rspo1, RSPO, R-spondin 1, R-spondin, Rspondin, CRISTIN3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RSPO1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RSPO1 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized RSPO1in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SRGIKGKRQR RISAEGSQAC AKGCELCSEV NGCLKCSPKL FILLERNDIR QVGVCLPSCP PGYFDARNPD MNKCIKCKIE HCEACFSHNF CTKCKEGLYL HKGRCYPACP EGSSAANGTM ECSSPAQCEM SEWSPWGPCS KKQQLCGFRR GSEERTRRVL HAPVGDHAAC SDTKETRRCT VRRVPCPEGQ KRRKGGQGRR ENANRNLARK ESKEAGAGSR RRKGQQQQQQ QGTVGPLTSA GPA.

    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.

    R Spondin 1 Human
  • View Data Sheet

    Name :

    UBXN2B Human

    Description:

    UBX Domain Protein 2B Human Recombinant

    UBX domain-containing protein 2B, p37, NSFL1 cofactor p37, p97 cofactor p37, UBXN2B.

    Product # :

    PRO-1512

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    UBXN2B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-331) and having a molecular mass of 39.5 kDa. UBXN2B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBXN2B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBX Domain Protein 2B (UBXN2B) is a 331 amino acid protein which comprises one UBX domain and one SEP domain. UBXN2B is essential for ER and Golgi biogenesis and also takes a place in their maintenance during interphase, as well as their reassembly at the end of mitosis. Through interaction with VCP, UBXN2B forms a complex that has membrane fusion activity.

    • Synonyms

      UBX domain-containing protein 2B, p37, NSFL1 cofactor p37, p97 cofactor p37, UBXN2B.

    • 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 MGSMAEGGGP EPGEQERRSS GPRPPSARDL QLALAELYED EVKCKSSKSN RPKATVFKSP RTPPQRFYSS EHEYSGLNIV RPSTGKIVNE LFKEAREHGA VPLNEATRAS GDDKSKSFTG GGYRLGSSFC KRSEYIYGEN QLQDVQILLK LWSNGFSLDD GELRPYNEPT NAQFLESVKR GEIPLELQRL VHGGQVNLDM EDHQDQEYIK PRLRFKAFSG EGQKLGSLTP EIVSTPSSPE EEDKSILNAV VLIDDSVPTT KIQIRLADGS RLIQRFNSTH RILDVRNFIV QSRPEFAALD FILVTSFPNK ELTDESLTLL EADILNTVLL QQLK.

    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.

    Ubxn2B Human
  • View Data Sheet

    Name :

    NCL Human

    Description:

    Nucleolin Human Recombinant

    Nucleolin, Protein C23, NCL, C23.

    Product # :

    PRO-1508

    Price :

    Quantity :

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    More Info

    • description
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    Description

    Nucleolin Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing the C-terminal section of the human nucleolin and missing the N-terminal histone-binding part of nucleolin, having a calculated molecular mass of 55,162 Dalton. NCL is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    NCL is supplied in 20mM HEPES pH-7.3, 600mM NaCl, 0.3mM Tris(2-carboxyethyl)phosphine (TCEP) and 25% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.

    • Synonyms

      Nucleolin, Protein C23, NCL, C23.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

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

    Ncl Human
  • View Data Sheet

    Name :

    Secretin Human

    Description:

    Secretin Human

    Product # :

    HOR-273

    Price :

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    • description
    • formulation
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    • More Info

    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

    • 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.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • 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.

    Secretin Human
  • View Data Sheet

    Name :

    Thymosin beta 4

    Description:

    Thymosin β4

    Thymosin beta-4. TB500, TB-500

    Product # :

    HOR-275

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    Description

    Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.

    • Synonyms

      Thymosin beta-4. TB500, TB-500

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.

    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.

    Thymosin Beta 4
  • View Data Sheet

    Name :

    TIPIN Human

    Description:

    TIMELESS Interacting Protein Human Recombinant

    TIMELESS Interacting Protein, CSM3 Homolog.

    Product # :

    PRO-1710

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    Description

    TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.

    • Synonyms

      TIMELESS Interacting Protein, CSM3 Homolog.

    • 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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR

    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.

    Tipin Human
  • View Data Sheet

    Name :

    UBE2B Human

    Description:

    Ubiquitin Conjugating Enzyme E2B Human Recombinant

    Ubiquitin-conjugating enzyme E2 B, EC 6.3.2.19, Ubiquitin-protein ligase B, Ubiquitin carrier protein B, HR6B, hHR6B, E2-17 kDa UBC2, HHR6B, RAD6B, E2-17kDa, UBE2B.

    Product # :

    ENZ-340

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    Description

    Ubiquitin Conjugating Enzyme E2B Human Recombinant produced in E.coli is a 19 kDa protein containing 166 amino acids.The UE2B protein contains 6xHis tag and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated (1 mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.

    Purity

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

    More Info

    • Introduction

      This E2 enzyme encodes for the human homolog of the yeast DNA repair gene RAD6, which is induced by DNA damaging agents. UBE2B can conjugate ubiquitin to histone H2A in an E3- independent manner in vitro, and is essential for the multi-ubiquitination and degradation of N-end rule substrates. Additionally, UBE2B may have a role in sepsis-induced muscle protein proteolysis and cancer-induced cachexia.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 B, EC 6.3.2.19, Ubiquitin-protein ligase B, Ubiquitin carrier protein B, HR6B, hHR6B, E2-17 kDa UBC2, HHR6B, RAD6B, E2-17kDa, UBE2B.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized UBE2B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2B 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 UBE2B in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHAMGQLRSMSTPARRRLMRDFKRLQEDPPVGVSGAPSENN
      IMQWNAVIFGPEGTPFEDGTFKLVIEFSEEYPNKPPTVRFLSKMFHPNVY
      ADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNSPANSQAAQLYQE
      NKREYEKRVSAIVEQSWNDS.

    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.

    Ube2B Human
  • View Data Sheet

    Name :

    TPK1 Human

    Description:

    Thiamin Pyrophosphokinase 1 Human Recombinant

    Thiamin pyrophosphokinase 1, hTPK1, Placental protein 20, PP20, Thiamine pyrophosphokinase 1, TPK1, THMD5.

    Product # :

    PKA-023

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    Description

    TPK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-243 a.a.) and having a molecular mass of 29.8kDa.TPK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPK1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thiamin pyrophosphokinase 1 (TPK1) is a homodimer which catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. TPK1 is found in the heart, kidney, testis, small intestine and peripheral blood leukocytes, and at very low levels in a variety of tissues. TPK1 gene defects cause the thiamine metabolism dysfunction syndrome type 5, episodic encephalopathy type (THMD5), which is an autosomal recessive metabolic disorder due to an inborn error of thiamine metabolism.

    • Synonyms

      Thiamin pyrophosphokinase 1, hTPK1, Placental protein 20, PP20, Thiamine pyrophosphokinase 1, TPK1, THMD5.

    • 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 MGSHMEHAFT PLEPLLSTGN LKYCLVILNQ PLDNYFRHLW NKALLRACAD GGANRLYDIT EGERESFLPE FINGDFDSIR PEVREYYATK GCELISTPDQ DHTDFTKCLK MLQKKIEEKD LKVDVIVTLG GLAGRFDQIM ASVNTLFQAT HITPFPIIII
      QEESLIYLLQ PGKHRLHVDT GMEGDWCGLI PVGQPCMQVT TTGLKWNLTN DVLAFGTLVS TSNTYDGSGV VTVETDHPLL WTMAIKS.

    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.

    Tpk1 Human
  • View Data Sheet

    Name :

    ErbB4 Human

    Description:

    Tyrosine Kinase ErbB-4 Human Recombinant

    Receptor tyrosine-protein kinase erbB-4, Proto-oncogene-like protein c-ErbB-4, Tyrosine kinase-type cell surface receptor HER4, p180erbB4, 4ICD, E4ICD, s80HER4, ERBB4, HER4, receptor tyrosine-protein kinase erbB-4 isoform JM-a/CVT-1, receptor tyrosine-protein kinase erbB-4, tyrosine kinase-type cell surface receptor HER4, avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4, proto-oncogene-like protein c-ErbB-4, ALS19, v-erb-a erythroblastic leukemia viral oncogene homolog 4, v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4, human epidermal growth factor receptor 4.

    Product # :

    PKA-128

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    Description

    ErbB4 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 863 amino acids (26-649 a.a) and having a molecular mass of 96.6 kDa.ErbB4 is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The ErbB4 solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human NRG1(CAT# cyt-1186). The ED50 range ≤ 0.2 ug/ml.

    More Info

    • Introduction

      Tyrosine Kinase ErbB-4 (ErbB4) is a receptor tyrosine kinase that is a member of the epidermal growth factor receptor family whose members play a role as receptors for the EGF family of growth factors. ErbB4is a single-pass type I transmembrane protein with multiple furin-like cysteine rich domains,PDZ domain binding motif, a tyrosine kinase domain and a phosphotidylinositol-3 kinase binding site. ErbB4binds its ligands with low affinity and is expressed in normal skeletal muscle, heart, pituitary, brain and some breast carcinomas. Monomeric ErbB4 takes part in neuronal development and development of the heart and cancer.

    • Synonyms

      Receptor tyrosine-protein kinase erbB-4, Proto-oncogene-like protein c-ErbB-4, Tyrosine kinase-type cell surface receptor HER4, p180erbB4, 4ICD, E4ICD, s80HER4, ERBB4, HER4, receptor tyrosine-protein kinase erbB-4 isoform JM-a/CVT-1, receptor tyrosine-protein kinase erbB-4, tyrosine kinase-type cell surface receptor HER4, avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4, proto-oncogene-like protein c-ErbB-4, ALS19, v-erb-a erythroblastic leukemia viral oncogene homolog 4, v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4, human epidermal growth factor receptor 4.

    • 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

      QSVCAGTENK LSSLSDLEQQ YRALRKYYEN CEVVMGNLEI TSIEHNRDLS FLRSVREVTG YVLVALNQFR YLPLENLRII RGTKLYEDRY ALAIFLNYRK DGNFGLQELG LKNLTEILNG GVYVDQNKFL CYADTIHWQD IVRNPWPSNL TLVSTNGSSG CGRCHKSCTG RCWGPTENHC QTLTRTVCAE QCDGRCYGPY VSDCCHRECA GGCSGPKDTD CFACMNFNDS GACVTQCPQT FVYNPTTFQL EHNFNAKYTY GAFCVKKCPH NFVVDSSSCV RACPSSKMEV EENGIKMCKP CTDICPKACD GIGTGSLMSA QTVDSSNIDK FINCTKINGN LIFLVTGIHG DPYNAIEAID PEKLNVFRTV REITGFLNIQ SWPPNMTDFS VFSNLVTIGG RVLYSGLSLL ILKQQGITSL QFQSLKEISA GNIYITDNSN LCYYHTINWT TLFSTINQRI VIRDNRKAEN CTAEGMVCNH LCSSDGCWGP GPDQCLSCRR FSRGRICIES CNLYDGEFRE FENGSICVEC DPQCEKMEDG LLTCHGPGPD NCTKCSHFKD GPNCVEKCPD GLQGANSFIF KYADPDRECH PCHPNCTQGC NGPTSHDCIY YPWTGHSTLP QHARLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH

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

    Erbb4 Human
  • View Data Sheet

    Name :

    Aprotinin Protein

    Description:

    Aprotinin

    Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.

    Product # :

    PRO-285

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    Description

    Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.

    Source

    Bovine Lung.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    More Info

    • Introduction

      Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).

    • Synonyms

      Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Specific Activity

      5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/mg.

    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.

    Bpti
  • View Data Sheet

    Name :

    IL 11 Human, Pichia

    Description:

    Interleukin-11 Human Recombinant, Pichia

    Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    Product # :

    CYT-013

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    Description

    IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    IL11 was Lyophilized from a 0.2 µm filtered concentrated solution of 20mM PB, pH7.2 and 2% Glycine buffer.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin -11 in sterile 18MΩ-cm H2O 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 Gly-Pro-Pro-Pro-Gly.

    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 11 Human Pichia
  • View Data Sheet

    Name :

    PAK4 Human

    Description:

    p21 Activated Kinase 4 Human Recombinant

    PAK-4, p21 (CDKN1A)-Activated Kinase 4, p21-Activated Kinase 4, Serine/threonine-protein kinase PAK 4, KIAA1142, PAK4.

    Product # :

    PKA-259

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    Description

    PAK4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 628 amino acids (1-591 a.a.) and having a molecular mass of 68.3 kDa.PAK4 is fused to 37 amino acid His-Tag at N-terminus and is purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The PAK4 protein (0.5mg/ml) contains 25mM HEPES pH-7.5, 150mM NaCl, 5mM MgCl2 and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PAK4 is part of the group B family of p21-activated kinases (PAK). It's known as an effector protein for cell division cycle 42(Cdc42) and protein that plays an important role in regulating cytoskeletal organization and cell morphology. PAK4 expression is eminent in many cancer cell lines, and is involved in tumorigenesis. PAK proteins are significant effectors that associate Rho GTPases to cytoskeleton reorganization and nuclear signaling. PAK proteins are targets for the small GTP binding proteins Cdc42 and Rac and have been implicated in a wide range of biological activities. PAK4 cooperates specifically with the GTP-bound form of Cdc42Hs and weakly activates the JNK family of MAP kinases. PAK4 is a mediator of filopodia formation and is involved in the reorganization of the actin cytoskeleton. PAK4 activates the JNK pathway. PAK4 phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments.

    • Synonyms

      PAK-4, p21 (CDKN1A)-Activated Kinase 4, p21-Activated Kinase 4, Serine/threonine-protein kinase PAK 4, KIAA1142, PAK4.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMFG KRKKRVEISA PSNFEHRVHT GFDQHEQKFT GLPRQWQSLI EESARRPKPL VDPACITSIQ PGAPKTIVRG SKGAKDGALT LLLDEFENMS VTRSNSLRRD SPPPPARARQ ENGMPEEPAT TARGGPGKAG SRGRFAGHSE AGGGSGDRRR AGPEKRPKSS REGSGGPQES SRDKRPLSGP DVGTPQPAGL ASGAKLAAGR PFNTYPRADT DHPSRGAQGE PHDVAPNGPS AGGLAIPQSS SSSSRPPTRA RGAPSPGVLG PHASEPQLAP PACTPAAPAV PGPPGPRSPQ REPQRVSHEQ FRAALQLVVD PGDPRSYLDN FIKIGEGSTG IVCIATVRSS GKLVAVKKMD LRKQQRRELL FNEVVIMRDY QHENVVEMYN
      SYLVGDELWV VMEFLEGGAL TDIVTHTRMN EEQIAAVCLA VLQALSVLHA QGVIHRDIKS DSILLTHDGR VKLSDFGFCA QVSKEVPRRK SLVGTPYWMA PELISRLPYG PEVDIWSLGI MVIEMVDGEP PYFNEPPLKA MKMIRDNLPP RLKNLHKVSP SLKGFLDRLL VRDPAQRATA AELLKHPFLA KAGPPASIVP LMRQNRTR.

    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.

    Pak4 Human
  • View Data Sheet

    Name :

    MAPK13 Human

    Description:

    Mitogen-Activated Protein Kinase 13 Human Recombinant

    Mitogen-activated protein kinase 13, PRKM13, SAPK4, p38delta, Mitogen-activated protein kinase p38 delta, Stress-activated protein kinase 4, MAP kinase 13, MAP kinase p38 delta, EC 2.7.11.24.

    Product # :

    PKA-273

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    Description

    MAPK13 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-365) and having a molecular mass of 44.2 kDa.MAPK13 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MAPK13 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPK13 belongs to the MAP kinase family. MAP kinases perform as an incorporation point for various biochemical signals. MAP kinases take part in an extensive range of cellular courses like differentiation, development, transcription regulation and proliferation. MAPK13 is phosphorylated by MKK6 as a reaction to cytokines and cellular stresses.

    • Synonyms

      Mitogen-activated protein kinase 13, PRKM13, SAPK4, p38delta, Mitogen-activated protein kinase p38 delta, Stress-activated protein kinase 4, MAP kinase 13, MAP kinase p38 delta, EC 2.7.11.24.

    • 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 MSLIRKKGFY KQDVNKTAWE LPKTYVSPTH VGSGAYGSVC SAIDKRSGEK VAIKKLSRPF QSEIFAKRAY RELLLLKHMQ HENVIGLLDV FTPASSLRNF YDFYLVMPFM QTDLQKIMGM EFSEEKIQYL VYQMLKGLKY IHSAGVVHRD LKPGNLAVNE DCELKILDFG LARHADAEMT GYVVTRWYRA PEVILSWMHY NQTVDIWSVG CIMAEMLTGK TLFKGKDYLD QLTQILKVTG VPGTEFVQKL NDKAAKSYIQ SLPQTPRKDF TQLFPRASPQ AADLLEKMLE LDVDKRLTAA QALTHPFFEP FRDPEEETEA QQPFDDSLEH EKLTVDEWKQ HIYKEIVNFS PIARKDSRRR SGMKL.

    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.

    Mapk13 Human
  • View Data Sheet

    Name :

    RPL26 Human

    Description:

    Ribosomal Protein L26 Human Recombinant

    L26, Ribosomal Protein L26, 60S Ribosomal Protein L26.

    Product # :

    PRO-1538

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    Description

    RPL26 Human Recombinant produced in E. coli is a single polypeptide chain containing 168 amino acids (1-145) and having a molecular mass of 19.6kDa. RPL26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPL26 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribosomal Protein L26 (RPL26) is a ribosomal protein which is a component of the 60S subunit (the large subunit of the ribosome). RPL26 is a part of the L24P family of ribosomal proteins which is located in the cytoplasm. There are numerous processed pseudogenes of RPL26 dispersed through the genome as usual for genes encoding ribosomal proteins.

    • Synonyms

      L26, Ribosomal Protein L26, 60S Ribosomal Protein L26.

    • 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 MGSMKFNPFV TSDRSKNRKR HFNAPSHIRR KIMSSPLSKE LRQKYNVRSM PIRKDDEVQV VRGHYKGQQI GKVVQVYRKK YVIYIERVQR EKANGTTVHV GIHPSKVVIT RLKLDKDRKK ILERKAKSRQ VGKEKGKYKE ETIEKMQE.

    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.

    Rpl26 Human
  • 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.

    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.

    Selank
  • View Data Sheet

    Name :

    CXCL4 Variant 1 Human

    Description:

    Platelet Factor-4 Variant 1 Human Recombinant

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-243

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    Description

    CXCL4 Variant-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized without additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets . Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily. Human PF4 is used for the proof of induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.

    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.

    Cxcl4 Variant 1
  • View Data Sheet

    Name :

    Darbepoetin

    Description:

    Darbepoetin-Alpha Human Recombinant

    Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    Product # :

    CYT-1263

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    Description

    Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells(CHO).

    Formulation

    Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

    More Info

    • Introduction

      Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.

    • Synonyms

      NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.

    • Background

      What is the molecular weight/Mw of DARBEPOETIN Protein?
      DARBEPOETIN Protein has a total Mw of 38.5kDa.

      What is the source or expression system of DARBEPOETIN Protein?
      Chinese Hamster Ovary Cells(CHO).

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

      What is the Biological Activity of DARBEPOETIN Protein?
      The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

      What is the amino acid sequence of DARBEPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD

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

      What is the endotoxin level for DARBEPOETIN Protein?
      The endotoxin level is minimal, DARBEPOETIN 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.

    Darbepoetin
  • View Data Sheet

    Name :

    Prolactin Human

    Description:

    Prolactin Human Recombinant

    Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    Product # :

    CYT-267

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    Description

    Prolactin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 23007 Dalton. The Prolactin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of rat lymphoma, Nb2-11 was found to be < 0.065ng/ml corresponding to a Specific Activity of 15,385,000IU/mg.

    More Info

    • Introduction

      Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

    • Synonyms

      Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Pro-Ile-Cys.

    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.

    Prolactin Human
  • View Data Sheet

    Name :

    PLA2G7 Human, HEK

    Description:

    Secreted Phospholipase A2-VII Human Recombinant, HEK

    Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.

    Product # :

    ENZ-736

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    Description

    Recombinant Human PLA2G7 produced in HEK293 cells is a polypeptide chain (22-441 a.a), fused to an 8 amino acid His-tag at C-terminus, containing a total of 428 amino acids. PLA2G7 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The PLA2G7 is supplied as a 0.2µm filtered solution in 20mM HAc-NaCl, 150mM NaCl and 10% Glycerol, pH 4.5.

    Purity

    Greater than 95% as determined by SEC-HPLC and SDS-PAGE.

    More Info

    • Introduction

      PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
      PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
      PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
      PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population.

    • Synonyms

      Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.

    • 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.Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      FDWQYINPVAHMKSSAWVNKIQVLMAAASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPS
      QDNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNILRLLFGSMTTPANWNSPLRPGEKYPLVVFSHGL
      GAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWLYLRTLKQEEETHIRN
      EQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLSE
      DQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVH
      QNFADFTFATGKIIGHMLKLKGDIDSNAAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENLI
      PGTNINTTNQHIMLQNSSGIEKYNVDHHHHHH.

    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.

    Pla2G7 Human Hek
  • View Data Sheet

    Name :

    HPCAL1 Human

    Description:

    Hippocalcin-Like 1 Human Recombinant

    Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3, VILIP-3

    Product # :

    PRO-254

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    Description

    HPCAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213amino acids (1-193a.a.) and having a molecular wieght of 24.4kDa. The HPCAL1 is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HPCAL1 protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 1mM DTT 0.2M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.

    • Synonyms

      Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3,
      VILIP-3

    • 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 MGKQNSKLRP EVLQDLRENT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD ASKFAEHVFR TFDTNGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA SQF

    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.

    Hpcal1 Human
  • View Data Sheet

    Name :

    ORAOV1 Human

    Description:

    Oral Cancer Overexpressed 1 Human Recombinant

    Oral cancer-overexpressed protein 1, Tumor-amplified and overexpressed sequence 1, ORAOV1, TAOS1.

    Product # :

    PRO-1092

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    Description

    ORAOV1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (1-137 a.a) and having a molecular mass of 17.9kDa.ORAOV1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ORAOV1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Oral cancer-overexpressed protein 1 (ORAOV1) is a candidate oncogene in the 11q13 chromosomal region. Functional analyses showed that ORAOV1 was involved in the regulation of HeLa cell growth via its effect on cell cycle and apoptosis. ORAOV1 is widely expressed; it has a high expression in the placenta, kidney and skeletal muscle. ORAOV1 is amplified and overexpressed in oral cancer cells.

    • Synonyms

      Oral cancer-overexpressed protein 1, Tumor-amplified and overexpressed sequence 1, ORAOV1, TAOS1.

    • 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 MGSHMAGSQD IFDAIVMADE RFHGEGYREG YEEGSSLGVM EGRQHGTLHG AKIGSEIGCY QGFAFAWKCL LHSCTTEKDS RKMKVLESLI GMIQKFPYDD PTYDKLHEDL DKIRGKFKQF CSLLNVQPDF KISAEGSGLS F.

    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.

    Oraov1 Human
  • View Data Sheet

    Name :

    Thymalin

    Description:

    Thymulin

    Product # :

    HOR-047

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    Description

    Thymulin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 858 Dalton and a Molecular formula of C33H54N12O15.

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

    • Amino Acid Sequence

      Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.

    • Background

      Thymulin, a nonapeptide hormone, is produced primarily by the thymus gland and has been recognized for its pivotal role in the immune system. It plays a significant role in the maturation and differentiation of T lymphocytes, which are crucial for immune function. Beyond its immune-related functions, research has increasingly unveiled the diverse physiological roles of thymulin. This study aims to comprehensively investigate thymulin, shedding light on its immunological functions and exploring its potential applications in various aspects of health and medicine.

      The primary objective of this research is to elucidate the mechanisms underlying thymulin's role in immune regulation. In vitro and in vivo experiments will be conducted to explore thymulin's interactions with immune cells, its impact on T cell development and function, and its potential modulation of immune responses. Understanding these mechanisms is fundamental for harnessing thymulin's immunomodulatory properties.

      The second objective is to assess the clinical relevance of thymulin in immune-related disorders. Clinical trials and studies involving individuals with autoimmune diseases, immunodeficiencies, and age-related immune decline will be conducted to evaluate the potential therapeutic applications of thymulin. These investigations may offer insights into the use of thymulin as an immunomodulatory agent in various clinical settings.

      The third objective is to explore the broader implications of thymulin in health and medicine. Research will investigate its potential roles in areas beyond immunology, such as neuroprotection, wound healing, and tissue regeneration. Understanding the multifaceted properties of thymulin may open new avenues for therapeutic interventions in various medical specialties.

      By delving into the diverse functions of thymulin, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may have implications for the development of innovative approaches in immunology and healthcare, ultimately benefiting patients affected by immune-related disorders and other medical conditions.

      What is the molecular weight/Mw of THYMALIN Protein?
      THYMALIN Protein has a total Mw of 0.85kDa.

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

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

      What is the amino acid sequence of THYMALIN Protein?
      Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.

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

      What is the endotoxin level for THYMALIN Protein?
      The endotoxin level is minimal, THYMALIN 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.

    Thymulin
  • View Data Sheet

    Name :

    SRGN Human

    Description:

    Serglycin Human Recombinant

    Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.

    Product # :

    PRO-965

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    SRGN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (28-158) and having a molecular mass of 17.4 kDa (Molecular weight on SDS-PAGE will appear higher).SRGN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.

    • Synonyms

      Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.

    • 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 MGSHMYPTRR ARYQWVRCNP DSNSANCLEE KGPMFELLPG ESNKIPRLRT DLFPKTRIQD LNRIFPLSED YSGSGFGSGS GSGSGSGSGF LTEMEQDYQL VDESDAFHDN LRSLDRNLPS DSQDLGQHGL EEDFML.

    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.

    Srgn Human
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