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Search results

1000 results found for “dead box protein”

Name

Description

Product #

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  • View Data Sheet

    Name :

    EDF1 Human

    Description:

    Endothelial Differentiation-Related Factor 1 Human Recombinant

    EDF-1, MBF1, Multiprotein-bridging factor 1.

    Product # :

    PRO-494

    Price :

    Quantity :

    Shipping Method :

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    Description

    EDF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-148 a.a.) and having a molecular mass of 17.4 kDa. The EDF1 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5 mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EDF1 controls endothelial cell differentiation. EDF1 has a role as a bridging protein that interconnects regulatory proteins and the basal transcriptional machinery, thus modulating the transcription of genes that take part in endothelial differentiation. EDF1 binds calmodulin through its IQ domain and controls nitric oxide synthase activity via calmodulin sequestration in the cytoplasm. EDF1 is localized in adult liver, heart, adipose tissues, intestine and pancreas.

    • Synonyms

      EDF-1, MBF1, Multiprotein-bridging factor 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV LGKIERAIGL KLRGKDIGKP IEKGPRAKLE HHHHHH.

    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.

    Edf1 Human
  • View Data Sheet

    Name :

    Leptin Receptor Chicken

    Description:

    Leptin Receptor Chicken Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    Product # :

    CYT-509

    Price :

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    Description

    Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    • Physical Appearance

      Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.

    • Stability

      Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of Leptin Binding Domain as a Reference Standard.

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

    Leptin Receptor Chicken
  • View Data Sheet

    Name :

    SOD Human

    Description:

    Superoxide Dismutase Human Recombinant

    Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.

    Product # :

    PRO-286

    Price :

    Quantity :

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    • description
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    Description

    Recombinant Human Cu/Zn Superoxide Dismutase produced in E.Coli is a non-glycosylated homodimeric polypeptide chain containing 2 x 153 amino acids and having a total molecular mass of 31.6kDa.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The potency per mg was tested by Pyrogallic Acid method and was found to be more than 3,000 Units/mg.

    More Info

    • Introduction

      Human Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. SOD1 binds copper and zinc ions and is 1 of 3 isozymes accountable for destroying free superoxide radicals in the body. The encoded protein neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis.

    • Synonyms

      Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      ATKAVCVLKG DGPVQGIINF EQKESNGPVK VWGSIKGLTE GLHGFHVHEF GDNTAGCTSA GPHFNPLSRK HGGPKDEERH VGDLGNVTAD KDGVADVSIE DSVISLSGDH CIIGRTLVVH EKADDLGKGG NEESTKTGNA GSRLACGVIG IAQ.

    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.

    Sod Human
  • View Data Sheet

    Name :

    DCTN2 (1-406) Human

    Description:

    Dynactin 2 (1-406 a.a.) Human Recombinant

    DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.

    Product # :

    PRO-1820

    Price :

    Quantity :

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    • description
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    Description

    Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 429 amino acids (1-406 a.a) and having a molecular mass of 47.2kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.

    • Synonyms

      DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.

    • 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 MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAFA QELEELTSTS VEHIIVNPNA AYDKFKDKRV GTKGLDFSDR IGKTKRTGYE SGEYEMLGEG LGVKETPQQK YQRLLHEVQE LTTEVEKIKT TVKESATEEK LTPVLLAKQL AALKQQLVAS HLEKLLGPDA AINLTDPDGA LAKRLLLQLE ATKNSKGGSG GKTTGTPPDS SLVTYELHSR PEQDKFSQAA KVAELEKRLT ELETAVRCDQ DAQNPLSAGL QGACLMETVE LLQAKVSALD LAVLDQVEAR LQSVLGKVNE IAKHKASVED ADTQSKVHQL YETIQRWSPI ASTLPELVQR LVTIKQLHEQ AMQFGQLLTH LDTTQQMIAN SLKDNTTLLT QVQTTMRENL ATVEGNFASI DERMKKLGK.

    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.

    Dctn2 1 406 Human
  • View Data Sheet

    Name :

    Leptin qA Human, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Human Recombinant

    Product # :

    CYT-1251

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/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

    Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C 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 Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports 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.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Human Qa Peg
  • View Data Sheet

    Name :

    Leptin Dog

    Description:

    Leptin Dog Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-506

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    Description

    Leptin Dog Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

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

    More Info

    • 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 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-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Dog
  • View Data Sheet

    Name :

    ARF3 Human

    Description:

    ADP-Ribosylation Factor 3 Human Recombinant

    ADP-ribosylation factor 3, ARF3.

    Product # :

    PRO-933

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    Description

    ARF3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8kDa.ARF3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARF3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-ribosylation factor 3 (ARF3) belongs to the human ARF gene family. This family encodes small guanine nucleotide-binding proteins which stimulate the ADP-ribosyltransferase activity of cholera toxin and have a role in vesicular trafficking and as activators of phospholipase D. ARF3 functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARF3 is involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. The ARF3 gene is comprised of 5 exons and 4 introns.

    • Synonyms

      ADP-ribosylation factor 3, ARF3.

    • 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 MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK K.

    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.

    Arf3 Human
  • View Data Sheet

    Name :

    HOXA9 Human

    Description:

    Homeobox A9 Human Recombinant

    Homeobox A9, HOX1G, Homeobox Protein Hox-1G, Homeodomain Protein HOXA9, Homeobox Protein Hox-A9, Homeo Box A9, HOX1.7, ABD-B, HOX1, HOXA9.

    Product # :

    PRO-1956

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    Description

    HOXA9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (1-272) and having a molecular mass of 32.6 kDa.HOXA9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HOXA9 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Homeobox A9 (HOXA9) is a member of the Abd-B homeobox family. The HOXA9 protein is a transcription factor with a key role in both haemopoiesis and leukaemia. High levels of HOXA9 expression in haemopoietic cells is a distinctive feature of acute myeloid leukaemia (AML), and may be sufficient to cause this disease. HOXA9 overexpression noticeably expands hematopoietic stem cells. The HOXA9 gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which regulates gene expression, morphogenesis, and differentiation. HOXA9 is a sequence-specific transcription factor which is part of a developmental regulatory system, which provides cells with specific positional identities on the anterior-posterior axis. HOXA9 is essential for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation.

    • Synonyms

      Homeobox A9, HOX1G, Homeobox Protein Hox-1G, Homeodomain Protein HOXA9, Homeobox Protein Hox-A9, Homeo Box A9, HOX1.7, ABD-B, HOX1, HOXA9.

    • 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 MGSMATTGAL GNYYVDSFLL GADAADELSV GRYAPGTLGQ PPRQAATLAE HPDFSPCSFQ SKATVFGASW NPVHAAGANA VPAAVYHHHH HHPYVHPQAP VAAAAPDGRY MRSWLEPTPG ALSFAGLPSS RPYGIKPEPL SARRGDCPTL DTHTLSLTDY ACGSPPVDRE KQPSEGAFSE NNAENESGGD KPPIDPNNPA ANWLHARSTR KKRCPYTKHQ TLELEKEFLF NMYLTRDRRY EVARLLNLTE RQVKIWFQNR RMKMKKINKD RAKDE.

    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.

    Hoxa9 Human
  • View Data Sheet

    Name :

    Anaplasma p44

    Description:

    Anaplasma phagocytophilum p44 Recombinant

    Product # :

    PRO-2566

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    Description

    Recombinant Anaplasma p44 produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 49kDa. Anaplasma p44 is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Anaplasma p44 is supplied at a 20mM HEPES buffer pH-8.0, 250mM NaCl and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Anaplasma p44 which belongs to the outer membrane antigen superfamily (OMP1/Msp2/p44), is a serodiagnostic antigen for HGA. Anaplasma p44 allows the bacterium to adhere to the host cell and prevents host immune surveillance.

    • Physical Appearance

      Sterile Filtered 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.

    • Immunological Functions

      1. Binds IgG- and IgM-type human antibodies. 2. Immunodot test with positive/negative samples.

    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.

    Anaplasma Phagocytophilum P44
  • View Data Sheet

    Name :

    GNAZ Human

    Description:

    Guanine Nucleotide Binding Protein Alpha Z Polypeptide Human Recombinant

    Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.

    Product # :

    PRO-1225

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    Description

    GNAZ Human Recombinant produced in E. coli is a single polypeptide chain containing 375 amino acids (1-355) and having a molecular mass of 43.0 kDa.GNAZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Guanine nucleotide-binding protein G(z) subunit alpha (GNAZ) belongs to the G protein subfamily which mediates signal transduction in pertussis toxin-insensitive systems. GNAZ has a role in maintaining the ionic balance of perilymphatic and endolymphatic cochlear fluids. G proteins are involved as modulators or transducers in a variety of transmembrane signaling systems.

    • Synonyms

      Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.

    • 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 MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG FNLEACKEYK PLIIYNAIDS LTRIIRALAA LRIDFHNPDR AYDAVQLFAL TGPAESKGEI TPELLGVMRR LWADPGAQAC FSRSSEYHLE DNAAYYLNDL ERIAAADYIP TVEDILRSRD MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLTICFPE YKGQNTYEEA AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC

    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.

    Gnaz Human
  • View Data Sheet

    Name :

    VEGF C Rat

    Description:

    Vascular Endothelial Growth Factor Related Protein Rat Recombinant

    VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L.

    Product # :

    CYT-262

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    Description

    Vascular Endothelial Growth Factor C Rat Recombinant contains 127 amino acids residues and was fused to a His- tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 15-20 kDa protein in SDS-PAGE under reducing conditions.

    Source

    Sf9, Insect Cells.

    Formulation

    Each mg of VEGF-C Rat contains 50mg BSA and PBS as buffer.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to stimulate phosphorylation of the VEGFR-3/FLT-4 receptor in porcine aortic endothelial cells. The ED50 for this effect is typically 200-300ng/ml corresponding to a Specific Activity of 3,334-5,000IU/mg.

    More Info

    • Introduction

      VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. The rat VEGFC cDNA encodes a pre-pro-protein of 416 amino acids residues.
      It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant rat VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT -4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant rat VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.

    • Synonyms

      VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      DTVKLAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGAATNTFFKP PCVSVYRCGGCCNSEGLQCMNTSTGYLSKTLFEITVPLSQGPKPVTISFA NHTSCRCMSKLDVYRQVHSIIHHHHHH.

    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.

    Vegf C Rat
  • View Data Sheet

    Name :

    Protein A, 434 a.a

    Description:

    Staphylococcal Protein A 434 a.a Recombinant

    Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    Product # :

    PRO-686

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    Description

    Recombinant Staphylococcal Protein A produced in E.Coli is a non-glycosylated, Polypeptide chain containing 434 amino acids (37-469 a.a.) and having a molecular mass of 48.1 kDa. Recombinant Staphylococcal Protein A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Protein-A protein solution contains 20mM Tris-HCl, pH-8 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).

    • Synonyms

      Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    • 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

      MAQHDEAQQN AFYQVLNMPN LNADQRNGFI QSLKDDPSQS ANVLGEAQKL NDSQAPKADA QQNNFNKDQQ SAFYEILNMP NLNEAQRNGFIQSLKDDPSQ STNVLGEAKK LNESQAPKAD NNFNKEQQNA FYEILNMPNL NEEQRNGFIQ SLKDDPSQSA NLLSEAKKLN ESQAPKADNK
      FNKEQQNAFY EILHLPNLNE EQRNGFIQSL KDDPSQSANL LAEAKKLNDA QAPKADNKFN KEQQNAFYEI LHLPNLTEEQ RNGFIQSLKDDPSVSKEILA EAKKLNDAQA PKEEDNNKPG KEDNNKPGKE DNNKPGKEDG NKPGKEDNKK PGKEDNKKPG KEDNKKPGKE DGNKPGKEDN
      KKPGKEDGNG VHVVKPGDTV NDIAKANGTT ADKIAADNKL ADKNMIKPGQ ELVVDKKQPA NHADANKAQA LPET.

    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.

    Protein A 434Aa
  • View Data Sheet

    Name :

    NCF1 Human

    Description:

    Neutrophil Cytosolic Factor 1 Human Recombinant

    NCF1A, NOXO2, p47phox, SH3PXD1A .

    Product # :

    PRO-488

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    Description

    NCF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-390 a.a.) and having a molecular mass of 45.7 kDa. The NCF1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NCF1 is a cytosolic subunit protein of neutrophil NADPH oxidase which a
      Multi-component enzyme that is activates production of superoxide anion. NCF1, along with NCF2 and a membrane bound cytochrome b558, is necessary for activation of the latent NADPH oxidase necessary for superoxide production. Mutations in this NCF1 have been related with chronic granulomatous disease.

    • Synonyms

      NCF1A, NOXO2, p47phox, SH3PXD1A .

    • 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

      MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDDVTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV VEHHHHHH.

    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.

    Ncf1 Human
  • 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

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    Description

    Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.

    More Info

    • 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
  • View Data Sheet

    Name :

    SGCB Human

    Description:

    Sarcoglycan Beta Human Recombinant

    Beta-sarcoglycan, Beta-SG, 43 kDa dystrophin-associated glycoprotein, 43DAG, A3b, LGMD2E, Sarcoglycan, Beta (43kDa Dystrophin-Associated Glycoprotein), Limb Girdle Muscular Dystrophy 2E (Non-Linked Families), SGC.

    Product # :

    PRO-2211

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    Description

    SGCB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (87-318 a.a) and having a molecular mass of 27.8kDa.SGCB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SGCB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer(pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Sarcoglycan Beta, also known as SGCB, is a part of the sarcoglycan family. SGCB belongs to the sarcoglycan complex which is a subcomplex of the dystrophin-glycoprotein complex that connects between the F-actin cytoskeleton and the extracellular matrix.

    • Synonyms

      Beta-sarcoglycan, Beta-SG, 43 kDa dystrophin-associated glycoprotein, 43DAG, A3b, LGMD2E, Sarcoglycan, Beta (43kDa Dystrophin-Associated Glycoprotein), Limb Girdle Muscular Dystrophy 2E (Non-Linked Families), SGC.

    • 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 MGSWAVIRIG PNGCDSMEFH ESGLLRFKQV SDMGVIHPLY KSTVGGRRNE NLVITGNNQP IVFQQGTTKL SVENNKTSIT SDIGMQFFDP RTQNILFSTD YETHEFHLPS GVKSLNVQKA STERITSNAT SDLNIKVDGR AIVRGNEGVF IMGKTIEFHM GGNMELKAEN SIILNGSVMV STTRLPSSSS GDQLGSGDWV RYKLCMCADG TLFKVQVTSQ NMGCQISDNP CGNTH.

    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.

    Sgcb Human
  • View Data Sheet

    Name :

    DCK Human

    Description:

    Deoxycytidine Kinase Human Recombinant

    Deoxycytidine kinase, DCK, MGC117410, MGC138632.

    Product # :

    PKA-313

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    Description

    DCK Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 296 amino acids (1-260 a.a.) and having a molecular mass of 34.6kDa. The DCK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DCK solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT, 0.1mM PMSF, 2mM EDTA and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DCK (Deoxycytidine kinase) is a key enzyme in the salvage of deoxyribonucleosides and in the activation of clinically relevant nucleoside analogues. DCK is responsible for the 5`-phosphorylation of purine and pyrimidine deoxynucleosides to the corresponding monophosphates using ATP or UTP as phosphate donors. Deficiency of the DCK enzyme activity is linked to resistance to antiviral and anticancer chemotherapeutic agents, whereas increased DCK enzyme activity is linked to increased activation of these compounds to cytotoxic nucleoside triphosphate derivatives.

    • Synonyms

      Deoxycytidine kinase, DCK, MGC117410, MGC138632.

    • Physical Appearance

      DCK is supplied as a 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMATP PKRSCPSFSA SSEGTRIKKI SIEGNIAAGK STFVNILKQL CEDWEVVPEP VARWCNVQST QDEFEELTMS QKNGGNVLQM MYEKPERWSF TFQTYACLSR IRAQLASLNG KLKDAEKPVL FFERSVYSDR YIFASNLYES ECMNETEWTI YQDWHDWMNN QFGQSLELDG IIYLQATPET CLHRIYLRGR NEEQGIPLEY LEKLHYKHES WLLHRTLKTN FDYLQEVPIL TLDVNEDFKD KYESLVEKVK EFLSTL.

    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.

    Dck Human
  • View Data Sheet

    Name :

    CTBP1 Human

    Description:

    C-Terminal Binding Protein 1 Human Recombinant

    EC 1.1.1, BARS, MGC104684, CTBP1, C-terminal-binding protein 1, CTBP.

    Product # :

    PRO-796

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    Description

    CTBP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 440 amino acids (1-440 a.a.) and having a molecular mass of 47.5kDa.CTBP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTBP1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTBP1 participates in controlling the equilibrium between tubular and stacked structures in the Golgi complex. CTBP1 functions in brown adipose tissue differentiation. CTBP1 has dehydrogenase activity. CTBP1 binds to the C-terminus of adenovirus E1A proteins. CTBP1 phosphoprotein is a transcriptional repressor and that takes part during cellular proliferation. CTBP1 & CTBP2 can dimerize and interact with a polycomb group protein complex which is involved in regulation of gene expression during development.

    • Synonyms

      EC 1.1.1, BARS, MGC104684, CTBP1, C-terminal-binding protein 1, CTBP.

    • 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

      MGSSHLLNKG LPLGVRPPIM NGPLHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV PAASVEETAD STLCHILNLY RRATWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG VERALGLQRV STLQDLLFHS DCVTLHCGLN EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT HWASMDPAVV HPELNGAAYR YPPGVVGVAP TGIPAAVEGI VPSAMSLSHG LPPVAHPPHA PSPGQTVKPE ADRDHASDQL.

    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.

    Ctbp1 Human
  • View Data Sheet

    Name :

    MYLPF Human

    Description:

    Myosin Light chain, Phosphorylatable, Fast Skeletal Muscle Human Recombinant

    Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    Product # :

    PRO-243

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    Description

    MYLPF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a) and having a molecular mass of 21.2kDa.MYLPF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYLPF protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin regulatory light chains, including MRCL3, MYLPF and MYL9, regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of myosin regulatory light chains, catalyzed by MLCK in the presence of calcium and calmodulin, increases the actin-activated myosin ATPase activity, thus regulating the contractile activity. MYLPF is vital for fast and slow skeletal muscle development.

    • Synonyms

      Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    • 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 MAPKRAKRRT VEGGSSSVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKKFL EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE.

    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.

    Mylpf Human
  • View Data Sheet

    Name :

    SPOCK3 Mouse

    Description:

    Sparc/Osteonectin 3 Mouse Recombinant

    Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.

    Product # :

    PRO-2328

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    Description

    SPOCK3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (22-436 a.a.) and having a molecular mass of 47.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).SPOCK3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SPOCK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Testican-3 (Spock3) is a nervous system-expressed heparan sulfate proteoglycan belonging to a subgroup of the BM-40/SPARC/osteonectin family, whose role of in brain development is unclear. Spock3 inhibits the processing of pro-matrix metalloproteinase 2(MMP-2) by MT1-MMP and MT3-MMP. Spock3 is mostly confined to the developmental stage of the brain.

    • Synonyms

      Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.

    • 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

      AAAAVAVAGG RSDGGNFLDE KQWLTTISQY DKEVGQWNKF RDEVEDDYFR TWNPGKPFDQ ALDPAKDPCL KTKCSRHKVC ITQDAQTALC ISHRRLTHSM KEVGGSHKQW RGLPSSTCKP CPIAYASPVC GSDGHSYSSQ CKLEYQACVL GKQISIKCEG RCPCPSDKSM NIGRNVKRAC
      SDLEFREVAN RLRDWFKALH ESGSQNKKTK ALLRPERSRF DTSILPICKD SLGWMFNRLD TNYDLLLDQS ELGSIYLDKN EQCTKAFFNS CDTYKDSLIS NNEWCYCFQR QQDPPCHTEL SNIQKRQGIK KLLGQYIPLC DEDGYYKPTQ CHGSVGQCWC VDRYGNEVVG SRINGVADCA
      IDFEISGDFA SGDFREWTDD EGEEDDIMND KDDIEDDDED EGDDDDDGDV HDGYILEHHH 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.

    Spock3 Mouse
  • View Data Sheet

    Name :

    TFB2M Human

    Description:

    Transcription Factor B2, Mitochondrial Human Recombinant

    Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.

    Product # :

    PRO-1259

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    Description

    TFB2M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (20-396 a.a) and having a molecular mass of 45.8kDa.TFB2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TFB2M protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription Factor B2, Mitochondrial (TFB2M) is an S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. In addition, TFB2M is essential for basal transcription of mitochondrial DNA, most likely via its interaction with POLRMT and TFAM. TFB2M promotes transcription independently of the methyltransferase activity. TFB2M like TFB1M, activates transcription of mitochondrial DNA more effectively, whilst having less methyltransferase activity.

    • Synonyms

      Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.

    • 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 MGSMAGRFCI LGSEAATRKH LPARNHCGLS DSSPQLWPEP DFRNPPRKAS KASLDFKRYV TDRRLAETLA QIYLGKPSRP PHLLLECNPG PGILTQALLE AGAKVVALES DKTFIPHLES LGKNLDGKLR VIHCDFFKLD PRSGGVIKPP AMSSRGLFKN LGIEAVPWTA DIPLKVVGMF PSRGEKRALW KLAYDLYSCT SIYKFGRIEV NMFIGEKEFQ KLMADPGNPD LYHVLSVIWQ LACEIKVLHM EPWSSFDIYT RKGPLENPKR RELLDQLQQK LYLIQMIPRQ NLFTKNLTPM NYNIFFHLLK HCFGRRSATV IDHLRSLTPL DARDILMQIG KQEDEKVVNM HPQDFKTLFE TIERSKDCAY KWLYDETLED R.

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    Tfb2M Human
  • View Data Sheet

    Name :

    MERTK Mouse

    Description:

    MER Proto-Oncogene Tyrosine Kinase Mouse Recombinant

    Tyrosine-protein kinase Mer, Proto-oncogene c-Mer, Receptor tyrosine kinase MerTK, Mertk, Mer.

    Product # :

    PKA-119

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    Description

    MERTK Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 718 amino acids (19-497 aa) and having a molecular mass of 79.2kDa.MERTK is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The MERTK solution (0.5 mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Proto-oncogene tyrosine-protein kinase MER is a protein, this enzyme is coded from the MERTK gene. This gene is a part of the TYRO3/AXL/MER receptor kinase group and encodes a transmembrane protein with two fibronectin type-III domains, two Ig-like C2-type (immunoglobulin-like) sites, and one tyrosine kinase site. Mutations in this gene have been correlated with interruption of the retinal pigment epithelium phagocytosis process and commencement of autosomal recessive retinitis pigmentosa.

    • Synonyms

      Tyrosine-protein kinase Mer, Proto-oncogene c-Mer, Receptor tyrosine kinase MerTK, Mertk, Mer.

    • 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

      GGTAEKWEET ELDQLFSGPL PGRLPVNHRP FSAPHSSRDQ LPPPQTGRSH PAHTAAPQVT
      STASKLLPPV AFNHTIGHIV LSEHKNVKFN CSINIPNTYQ ETAGISWWKD GKELLGAHHS
      ITQFYPDEEG VSIIALFSIA SVQRSDNGSY FCKMKVNNRE IVSDPIYVEV QGLPYFIKQP
      ESVNVTRNTA FNLTCQAVGP PEPVNIFWVQ NSSRVNEKPE RSPSVLTVPG LTETAVFSCE
      AHNDKGLTVS KGVHINIKVI PSPPTEVHIL NSTAHSILVS WVPGFDGYSP LQNCSIQVKE
      ADRLSNGSVM VFNTSASPHL YEIQQLQALA NYSIAVSCRN EIGWSAVSPW ILASTTEGAP
      SVAPLNITVF LNESNNILDI RWTKPPIKRQ DGELVGYRIS HVWESAGTYK ELSEEVSQNG
      SWAQIPVQIH NATCTVRIAA ITKGGIGPFS EPVNIIIPEH SKVDYAPSST PAPGNTDSM
      LEPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF
      NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT
      ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP
      PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH

    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.

    MERTK Mouse
  • View Data Sheet

    Name :

    CDNF Mouse

    Description:

    Cerebral Dopamine Neurotrophic Factor Mouse Recombinant

    Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.

    Product # :

    CYT-729

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    Description

    CDNF Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.

    More Info

    • Introduction

      CDNF is a member of the ARMET family and acts as a trophic factor for dopamine neurons. CDNF inhibits the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the dopaminergic function and inhibits the degeneration of dopaminergic neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.

    • Synonyms

      Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.

    • Background

      What is the molecular weight/Mw of CDNF Protein?
      CDNF Protein has a total Mw of 18.5kDa.

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

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

      What is the Biological Activity of CDNF Protein?
      CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.

      What is the amino acid sequence of CDNF Protein?
      QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.

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

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

    Cdnf Mouse
  • View Data Sheet

    Name :

    NECTIN3 Human

    Description:

    Nectin Cell Adhesion Molecule 3 Human Recombinant

    Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3. 

    Product # :

    PRO-2504

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    • More Info

    Description

    NECTIN3 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 355 amino acids (58-404 a.a.) and having a molecular mass of 39.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    NECTIN3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NECTIN3, also known as Nectin Cell Adhesion Molecule 3, is part of the nectin family. NECTIN3 is intended to initiate cell-cell adhesion to stimulate cell attachment and to allow subsequent formation of JAM-and cadherin-based intercellular junctions. NECTIN3 induces endocytosis-mediated down-regulation of PVR from the cell surface, which results in reduction of cell movement & proliferation. Following Nectin-3 activity adds strength to the junction through trans-interaction with various molecules.

    • Synonyms

      Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3.

    • 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

      GPIIVEPHVT AVWGKNVSLK CLIEVNETIT QISWEKIHGK SSQTVAVHHP QYGFSVQGEY QGRVLFKNYS LNDATITLHN IGFSDSGKYI CKAVTFPLGN AQSSTTVTVL VEPTVSLIKG PDSLIDGGNE TVAAICIAAT GKPVAHIDWE GDLGEMESTT TSFPNETATI ISQYKLFPTR FARGRRITCV VKHPALEKDI RYSFILDIQY APEVSVTGYD GNWFVGRKGV NLKCNADANP PPFKSVWSRL DGQWPDGLLA SDNTLHFVHP LTFNYSGVYI CKVTNSLGQR SDQKVIYISD PPTTTTLQPT IQWHPSTADI EDLATEPKKL PFPLSTLATI KDDTIATLEH HHHHH.

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    Nectin3 Human
  • View Data Sheet

    Name :

    ANXA3 Human

    Description:

    Annexin A3 Human Recombinant

    ANX3, ANXA3, Annexin-III, Lipocortin-3, Lipocortin-III, Annexin-3, Annexin A3, Placental anticoagulant protein III, PAP-III, 35-alpha calcimedin, Inositol 1,2-cyclic phosphate 2-phosphohydrolase.

    Product # :

    PRO-765

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    ANXA3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-323 a.a.) and having a molecular mass of 36.3 kDa. ANXA3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA3 protein solution contains 20mM Tris-HCl, pH-7.5, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ANXA3 is an inhibitor of phospholipase A2. ANXA3 possesses anti-coagulant properties. ANXA3 cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. ANXA3 is part of the annexin family which are members of the calcium-dependent phospholipid-binding protein family that are involved in the regulation of cellular growth and in signal transduction pathways. ANXA3 takes part as an anti-coagulation factor.

    • Synonyms

      ANX3, ANXA3, Annexin-III, Lipocortin-3, Lipocortin-III, Annexin-3, Annexin A3, Placental anticoagulant protein III, PAP-III, 35-alpha calcimedin, Inositol 1,2-cyclic phosphate 2-phosphohydrolase.

    • 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

      MASIWVGHRG TVRDYPDFSP SVDAEAIQKA IRGIGTDEKM LISILTERSN AQRQLIVKEY QAAYGKELKD DLKGDLSGHF EHLMVALVTP PAVFDAKQLK KSMKGAGTNE DALIEILTTR TSRQMKDISQ AYYTVYKKSL GDDISSETSG DFRKALLTLA DGRRDESLKV DEHLAKQDAQ ILYKAGENRW GTDEDKFTEI LCLRSFPQLK LTFDEYRNIS QKDIVDSIKG ELSGHFEDLL LAIVNCVRNT PAFLAERLHR ALKGIGTDEF TLNRIMVSRS EIDLLDIRTE FKKHYGYSLY SAIKSDTSGD YEITLLKICG GDD.

    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.

    Anxa3 Human
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