Search: 1000 results found for "hepatitis d"

Description:

Mouse Anti SARS Nucleocapsid Horseradish Peroxidase

Product # :

ANT-765

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Description

SARS Nucleoprotein HRP antibody clone PT3851 is specific for the nucleocapsid SARS-CoV protein and recognizes the nucleoprotein of SARS-CoV-2 by ELISA.

Formulation

1mg/ml in DPBS, 1% BSA and 0.1% Proclin 950.

Purity

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

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Introduction
SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.
Physical Appearance
Sterile Filtered liquid formulation.
Stability
Store at 4°C, stable for 2 weeks. For long-term storage, store at -20°C.
Immunogen
Recombinant protein fragment 1-49 a.a. of the SARS nucleoprotein.
Clone
PT3851
Applications
ELISA.
Isotype
Mouse IgG2b.
Type
Mouse antibody Monoclonal.
Purification Method
Protein A affinity purified.

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

Description:

Uroporphyrinogen Decarboxylase Human Recombinant

UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.

Product # :

ENZ-536

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Description

UROD Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 43 kDa. The UROD is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

UROD Human solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl, 1mM EDTA & 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
UROD is the fifth enzyme in the human heme biosynthetic pathway and is in charge for the transfer of uroporphyrinogen to coproporphyrinogen through the deletion of four carboxymethyl side chains. UROD Mutations and deficiency result in 3 autosomal disorders in humans: familial porphyria cutanea tarda (f-PCT), sporadic porphyria cutanea tarda (s-PCT) and hepatoerythropoietic porphyria (HEP).
Synonyms
UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.
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 MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT LQVNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH SRLLRQN.

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

Description:

Pfu-sso7d DNA Polymerase Recombinant

DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.

Product # :

ENZ-1202

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Description

Pfu-sso7d DNA Polymerase is derived from E. coli, having a molecular mass of 100 kDa. The Pfu-sso7d DNA Polymerase possesses the following activities: 5´→3´ DNA polymerase activity and 3´→5´ exonuclease activity. It generates blunt ends in the amplification products. The Pfu-ssod7 DNA Polymerase brings together a Pyrococcus furiosus DNA polymerase with a proc+essivity-enhancing domain Ssod7.

Source

Escherichia Coli.

Formulation

20mM Tris-HCl (pH 8.0), 50% glycerol, 0.1mM EDTA, 100mM KCl, 1mM DTT, 0.1% Tween20 and 0.1% NP-40.

Purity

Greater than 95 % as determined by SDS-PAGE analyses

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Synonyms
DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.
Physical Appearance
Sterile liquid formulation.
Stability
Store Pfu-sso7d DNA Polymerase 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.
Applications
It is applicable for amplification reaction of genomic DNA, cDNA, dU-containing DNA and crude samples as templates.
Background
The Pfu-sso7d DNA Polymerase preforms very well for all major PCR applications. The Pfu-sso7d DNA Polymerase generates long amplicons with accuracy and speed. The high fidelity makes the Pfu-sso7d DNA Polymerase a great choice for cloning. The error rate of Pfu-sso7d DNA Polymerase is approximately 50 fold lower than that of the Thermus aquaticus DNA polymerase. It generates blunt ends in the amplification products.
Unit Definition
1U of enzyme catalyzes the incorporation of 10nmol of dNTP into polynucleotide fraction in 30 minutes at 74°C.

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

Description:

CD4 (26-396) Human Recombinant, Sf9

CD4 Molecule, T-Cell Surface Antigen T4/Leu-3, CD4 Antigen (P55), T-Cell Surface Glycoprotein CD4, CD4 Receptor, CD4 Antigen, CD4mut.

Product # :

CYT-978

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Description

CD4 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 377 amino acids (26-396a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CD4 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

CD4 a protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CD4 is a cell-surface glycoprotein found on the mature helper T cells and immature thymocytes, as well as on monocytes and macrophages. (Some cytotoxic T cells have CD4 protein as well.) Normally, about 65% of T cells in the blood are CD4+ (have CD4 protein protruding from their membrane). A mature T cell with either have CD4 or CD8, but not both. During one stage of development T cells develop CD4 and CD8 receptors, but they eventually are differentiated in the thymus and become more specialized.
Synonyms
CD4 Molecule, T-Cell Surface Antigen T4/Leu-3, CD4 Antigen (P55), T-Cell Surface Glycoprotein CD4, CD4 Receptor, CD4 Antigen, CD4mut.
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
KKVVLGKKGD TVELTCTASQ KKSIQFHWKN SNQIKILGNQ GSFLTKGPSK LNDRADSRRS LWDQGNFPLI IKNLKIEDSD TYICEVEDQK EEVQLLVFGL TANSDTHLLQ GQSLTLTLES PPGSSPSVQC RSPRGKNIQG GKTLSVSQLE LQDSGTWTCT VLQNQKKVEF KIDIVVLAFQ KASSIVYKKE GEQVEFSFPL AFTVEKLTGS GELWWQAERA SSSKSWITFD LKNKEVSVKR VTQDPKLQMG KKLPLHLTLP QALPQYAGSG NLTLALEAKT GKLHQEVNLV VMRATQLQKN LTCEVWGPTS PKLMLSLKLE NKEAKVSKRE KAVWVLNPEA GMWQCLLSDS GQVLLESNIK VLPTWSTPVQ PHHHHHH.

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

Description:

P450 Oxidoreductase Human Recombinant

P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.

Product # :

ENZ-1186

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Description

POR Human Recombinant produced in Sf9 Insect cells is a single, glycosylated, polypeptide chain (43-677 a.a) containing a total of 642 amino acids, having a molecular mass of 73.0 kDa. POR is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 1,500 pmol/min/mg. Defined by the amount of enzyme that reduction of 1 pmole cytochrome-C by NADPH/min. at pH-8 25C.

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Synonyms
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
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
MLFRKKKEEV PEFTKIQTLT SSVRESSFVE KMKKTGRNII VFYGSQTGTA EEFANRLSKD AHRYGMRGMS ADPEEYDLAD LSSLPEIDNA LVVFCMATYG EGDPTDNAQD FYDWLQETDV DLSGVKFAVF GLGNKTYEHF NAMGKYVDKR LEQLGAQRIF ELGLGDDDGN LEEDFITWRE QFWPAVCEHF GVEATGEESS IRQYELVVHT DIDAAKVYMG EMGRLKSYEN QKPPFDAKNP FLAAVTTNRK LNQGTERHLM HLELDISDSK IRYESGDHVA VYPANDSALV NQLGKILGAD LDVVMSLNNL DEESNKKHPF PCPTSYRTAL TYYLDITNPP RTNVLYELAQ YASEPSEQEL LRKMASSSGE GKELYLSWVV EARRHILAIL QDCPSLRPPI DHLCELLPRL QARYYSIASS SKVHPNSVHI CAVVVEYETK AGRINKGVAT NWLRAKEPAG ENGGRALVPM FVRKSQFRLP FKATTPVIMV GPGTGVAPFI GFIQERAWLR QQGKEVGETL LYYGCRRSDE DYLYREELAQ FHRDGALTQL NVAFSREQSH KVYVQHLLKQ DREHLWKLIE GGAHIYVCGD ARNMARDVQN TFYDIVAELG AMEHAQAVDY IKKLMTKGRY SLDVWSHHHH HH.
Background
P450 Oxidoreductase (POR) is a vital enzyme that plays a crucial role in the electron transfer system, specifically in the cytochrome P450 (CYP) enzyme family. POR acts as an electron donor for various CYP enzymes involved in drug metabolism, steroid biosynthesis, and detoxification processes. This research aims to explore the function, regulation, and significance of POR protein in human cells, shedding light on its role in maintaining cellular homeostasis and drug metabolism.
Function of POR Protein:
POR protein serves as an essential component in the redox reactions of the CYP enzymes. It transfers electrons from NADPH to the CYP enzymes, allowing them to catalyze a wide range of reactions involved in the metabolism of endogenous compounds, drugs, and toxins. Through its electron transfer function, POR enables the activation or inactivation of substrates, contributing to the regulation of cellular processes such as hormone synthesis, drug clearance, and xenobiotic detoxification.
Regulation of POR Protein:
The expression and activity of POR protein are tightly regulated to ensure proper functioning of the CYP enzymes. Several factors influence POR expression, including genetic variations, environmental stimuli, and hormonal signals. Transcriptional regulation of POR involves binding of specific transcription factors to its promoter region. Additionally, post-translational modifications, such as phosphorylation and protein-protein interactions, modulate POR activity, influencing its electron transfer efficiency and interaction with CYP enzymes.
Role of POR Protein in Drug Metabolism:
One of the prominent functions of POR protein is its involvement in drug metabolism. POR collaborates with CYP enzymes in the biotransformation of a wide array of drugs, converting them into more soluble and easily excretable forms. The interplay between POR and CYP enzymes determines the pharmacokinetics and therapeutic efficacy of numerous drugs. Understanding the role of POR in drug metabolism is crucial for predicting drug-drug interactions, optimizing drug dosing, and minimizing the risk of adverse reactions.
Significance of POR Protein in Disease States:
Emerging evidence suggests that POR protein dysregulation can contribute to various disease states. Mutations in the POR gene have been linked to disorders such as Antley-Bixler syndrome and disordered steroidogenesis, highlighting the critical role of POR in development and endocrine function. Moreover, altered POR expression and activity have been implicated in drug resistance and toxicity, as well as in the pathogenesis of certain cancers.
Conclusion:
The investigation of P450 Oxidoreductase (POR) protein in human cells provides valuable insights into its function, regulation, and significance in various physiological and pathological processes. Understanding the interplay between POR and CYP enzymes is essential for deciphering drug metabolism pathways, predicting drug interactions, and developing personalized therapeutic strategies. Further research is warranted to unravel the intricate mechanisms governing POR activity and its potential as a therapeutic target.

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

Description:

Growth Hormone Human Recombinant, HEK

GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

CYT-091

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Description

Growth Hormone Human Recombinant produced in HEK cells is a non-glycosylated monomer, having a total molecular weight of 22kDa.The GH is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The GH was lyophilized from 1.13mg/ml in 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The activity was determined by the dose dependent stimulation of the proliferation of rat lymphoma line Nb2-11 cells (prolactin indicator cell line), the ED₅₀ is 0.1ng/ml.

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH 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 GH in sterile 1xPBS containing 0.1% endotoxin-free recombinant HSA.

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

Description:

DnaK Substrate Binding Domain E.Coli Recombinant

HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

Product # :

HSP-008

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Description

Recombinant DnaK Substrate Binding domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing (385-546 a.a.) 163 amino acids and having a molecular mass of 17.7 kDa.

Source

Escherichia Coli.

Formulation

The protein contains 25mM Tris-HCl, pH7.5, 2mM B-ME and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. Dnak(residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK(amino acid 508-638) was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.
Synonyms
HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
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
MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HST.

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

Description:

Glial-Derived Neurotrophic Factor Human Recombinant, Sf9

Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.

Product # :

CYT-1162

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Description

GDNF Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 113amino acids (109-211 aa) and having a molecular mass of 12.8kDa.GDNF is fused to an 10 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Glial cell-derived neurotrophic factor or GDNF is part of the GDNF group of ligands proteins. GDNF has a crucial part in numerous cell mechanisms such as neurite outgrowth, cell differentiation, cell survival and migration of cells. GDNF enhances neurons survival via GFRa receptors (mainly GFRa1). The mentioned neurons can die as a result from Parkinson's disease or ALS (amyotrophic lateral sclerosis). This protein takes part in the development of the spermatogenesis & kidney, also, it has a role in alcohol metabolism as ameliorating.
Synonyms
Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.
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
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH
Background
What is the molecular weight/Mw of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein has a total Mw of 12.8kDa.

What is the source or expression system of GDNF HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of GDNF HUMAN, SF9 Protein?
The biological functionality of GDNF HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of GDNF HUMAN, SF9 Protein?
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH

What applications can GDNF HUMAN, SF9 Protein be used in?
GDNF HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDNF HUMAN, SF9 Protein?
The endotoxin level is minimal, GDNF HUMAN, SF9 Protein was purified using conventional chromatography techniques.

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

Description:

Apolipoprotein-M Human Recombinant, HEK

G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

Product # :

CYT-026

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Description

APOM HEK Human Recombinant Protein is 20 kDa protein containing 179 amino acid residues of the APOM Human and 13 additional amino acid residues of flag Tag.

Source

HEK293.

Formulation

APOM Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 20mM TRIS and 50mM NaCl, pH 7.5.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
APOM is belongs to the lipocalin protein family and is associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it takes part in lipid transport.
Synonyms
G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Store lyophilized APOM Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted APOM Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
HVDYKDDDDK PAGCPEHSQL TTLGVDGKEF PEVHLGQWYF IAGAAPTKEE LATFDPVDNI VFNMAAGSAP MQLHLRATIR MKDGLCVPRK WIYHLTEGST DLRTEGRPDM KTELFSSSCP GGIMLNETGQ GYQRFLLYNR SPHPPEKCVE EFKSLTSCLD SKAFLLTPRN QEACELSNN
Applications
Cell culture and/or animal studies, ELISA and Western blotting.
Background
What is the molecular weight/Mw of APOM Protein?
APOM Protein has a total Mw of 20kDa.

What is the source or expression system of APOM Protein?
HEK293.

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

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

What is the amino acid sequence of APOM Protein?
HVDYKDDDDK PAGCPEHSQL TTLGVDGKEF PEVHLGQWYF IAGAAPTKEE LATFDPVDNI VFNMAAGSAP MQLHLRATIR MKDGLCVPRK WIYHLTEGST DLRTEGRPDM KTELFSSSCP GGIMLNETGQ GYQRFLLYNR SPHPPEKCVE EFKSLTSCLD SKAFLLTPRN QEACELSNN

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

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

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

Description:

Fibroblast Growth Factor-8 Human Recombinant, HEK

FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

Product # :

CYT-087

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Description

FGF-8 Human Recombinant is a single, glycosylated, polypeptide chain (23-215 a.a) containing a total of 204 amino acids and having a molecular mass of 23.7 kDa. FGF-8 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The FGF-8 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90% as obsereved by SDS-PAGE.

Biological Activity

The ED50 is ≤5 µg/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.

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Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
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
DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 23.7kDa.

What is the source or expression system of FGF8 Protein?
HEK.

What is the Purity of FGF8 Protein?
FGF8 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF8 Protein?
The ED50 is ≤5 µg/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.

What is the amino acid sequence of FGF8 Protein?
DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.

What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 Protein was purified using conventional chromatography techniques.

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

Description:

CD27 Human Recombinant, HEK

Tumor Necrosis Factor Receptor Superfamily Member 7, T-Cell Activation Antigen CD27, CD27 Molecule, CD27 Antigen, T Cell Activation Antigen S152, CD27L Receptor, TNFRSF7, S152, Tp55, T14.

Product # :

PRO-2751

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Description

CD27 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-191 a.a) containing a total of 411 amino acids, having a molecular mass of 46.2kDa. CD27 is fused to a 239 amino acid hIgG-His-Tag at C-terminus,and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The CD27 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

ED50 range is ≤ 0.8 ug/ml. Defined by its binding ability in a functional ELISA with Human CD27 Ligand/TNFSF7 (CAT# cyt-953).

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Introduction
CD27 belongs to the TNF-receptor superfamily. CD27 is necessary for initiation and long-term maintenance of T cell immunity. CD27 binds to ligand CD70, and has a crucial role in regulating B-cell activation and immunoglobulin synthesis. The CD27 receptor transduces signals which result in the activation of NF-kappaB and MAPK8/JNK. Adaptor proteins TRAF2 and TRAF5 mediate the signaling process of CD27. CD27-binding protein (SIVA), which is a proapoptotic protein, can bind to the CD27 receptor and is believed to have a significant role in the apoptosis induced by CD27.
Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 7, T-Cell Activation Antigen CD27, CD27 Molecule, CD27 Antigen, T Cell Activation Antigen S152, CD27L Receptor, TNFRSF7, S152, Tp55, T14.
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
ATPAPKSCPE RHYWAQGKLC CQMCEPGTFL VKDCDQHRKA AQCDPCIPGV SFSPDHHTRP HCESCRHCNS GLLVRNCTIT ANAECACRNG WQCRDKECTE CDPLPNPSLT ARSSQALSPH PQPTHLPYVS EMLEARTAGH MQTLADFRQL PARTLSTHWP PQRSLCSSDF IRLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H

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

Description:

Beta Defensin 116 Human Recombinant

Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.

Product # :

CYT-713

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Description

DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

sds-page

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Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
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 MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:

Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.
Introduction:

Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.
Production and Characterization:

Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.
Antimicrobial Properties:

BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.
Therapeutic Implications:

The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.
Conclusion:

Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.
What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.

What is the source or expression system of DEFB116 Protein?
Escherichia Coli.

What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.

What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.

What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 Protein was purified using conventional chromatography techniques.

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

Description:

Dengue Virus NS1 Subtype 3 Recombinant, Insect Cells

Product # :

DEN-031

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Description

Recombinant Dengue Virus NS1 Subtype 3 produced in Insect Cells is a polypeptide chain containing amino acids 775-1129 and having a molecular weight of approximately 50kDa. Dengue NS1 ST3 is purified by proprietary chromatographic technique.

Source

Insect cells.

Formulation

Dengue NS1 ST3 protein solution (1mg/ml) in 1xPBS, pH7.4, 0.1% Thimerosal, 5mM EDTA, 1µg/ml of Leupeptin, Aprotinin and Pepstatin A.

Purity

Protein is >95% pure as determined by 12.5% SDS-PAGE.

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Introduction
Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.
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.
Applications
Ag test control.

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

Description:

Interferon-alpha 2b 20kd-Pegylated Human Recombinant

Interferon alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

Product # :

CYT-034

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Description

Interferon-a 2b Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19269 Dalton. The Pegylated IFN-a 2b is produced by attaching a 20kDa mPEG-aldehyde to the N-terminal IFN alpha-2b. Interferon-a 2b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IFN-a 2b is supplied in solution (1.48mg/ml) containing 20mM Acetate Buffer (pH 6.0), 0.8%NaCl and 0.005% Polysorbate 80.

Purity

Greater than 97.0% as determined by SEC-HPLC.

Biological Activity

The specific activity as determined in a viral resistance assay using VSV-WISH cells was found to be 3,000,000 IU/mg.

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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. Interferon stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
Interferon alpha 2b, IFNA, INFA2, MGC125764, MGC125765.
Physical Appearance
Colorless, clear and transparent solution.
Stability
IFN alpha-2b PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in their packaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of IFN A 2B HUMAN, 20 KD PEG Protein?
IFN A 2B HUMAN, 20 KD PEG Protein has a total Mw of 19.2kDa.

What is the source or expression system of IFN A 2B HUMAN, 20 KD PEG Protein?
Escherichia Coli.

What is the Purity of IFN A 2B HUMAN, 20 KD PEG Protein?
IFN A 2B HUMAN, 20 KD PEG Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2B HUMAN, 20 KD PEG Protein?
The specific activity as determined in a viral resistance assay using VSV-WISH cells was found to be 3,000,000 IU/mg.

What is the amino acid sequence of IFN A 2B HUMAN, 20 KD PEG Protein?
IFN A 2B HUMAN, 20 KD PEG Protein is composed from 165 amino acids.

What applications can IFN A 2B HUMAN, 20 KD PEG Protein be used in?
IFN A 2B HUMAN, 20 KD PEG Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN A 2B HUMAN, 20 KD PEG Protein?
The endotoxin level is minimal, IFN A 2B HUMAN, 20 KD PEG Protein was purified using conventional chromatography techniques.

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

Description:

HA Mouse Antibody

Product # :

ANT-225

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formulation
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Description

Monoclonal antibodies are produced by immunizing mouse with synthetic peptide (YPYDVPDYA) coupled to KLH.

Formulation

1×PBS & 50% glycerol.

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Physical Appearance
Sterile filtered colorless solution.
Ig Subclass
Mouse IgG1.
Clone
PHASHG.
Applications
Western Blot, Immunoprecipitation.
Titer
Western Blotting: 1µg/ml.
Type
Mouse Antibody Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

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

Description:

DnaJ (Hsp40) homolog, subfamily B, member 2 Human Recombinant

DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, Heat shock 40 kDa protein 3, Heat shock protein J1, HSJ-1, DNAJB2, HSJ1, HSPF3.

Product # :

HSP-035

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Description

DNAJB2 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 300 amino acids (1-277 a.a.) and having a molecular mass of 33kDa. The DNAJB2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DNAJB2 solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
DnaJB2 is a member of the DnaJ family. The DnaJ family is one of the largest of all the chaperone families which has evolved with diverse cellular localization and functions. DnaJB2 are important mediators of proteolysis which are involved in the regulation of protein degradation, exocytosis and endocytosis. The DnaJ proteins play a significant role in the HSP70 chaperone machine by interacting with HSP70 to stimulate ATP hydrolysis. DnaJB2 is expressed almost solely in the brain, with the highest levels in the frontal cortex and hippocampus.
Synonyms
DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, Heat shock 40 kDa protein 3, Heat shock protein J1, HSJ-1, DNAJB2, HSJ1, HSPF3.
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 MGSMASYYEI LDVPRSASAD DIKKAYRRKA LQWHPDKNPD NKEFAEKKFK EVAEAYEVLS DKHKREIYDR YGREGLTGTG TGPSRAEAGS GGPGFTFTFR SPEEVFREFF GSGDPFAELF DDLGPFSELQ NRGSRHSGPF FTFSSSFPGH SDFSSSSFSF SPGAGAFRSV STSTTFVQGR RITTRRIMEN GQERVEVEED GQLKSVTING VPDDLALGLE LSRREQQPSV TSRSGGTQVQ QTPASCPLDS DLSEDEDLQL AMAYSLSEME AAGKKPADVF.

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

Description:

Eukaryotic Translation Elongation Factor 1 Delta Human Recombinant

Elongation factor 1-delta, EF-1-delta, Antigen NY-CO-4, EEF1D, EF1D, EF-1D, FP1047, FLJ20897.

Product # :

PRO-170

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Description

EEF1D Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 301 amino acids (1-281 a.a.) and having a molecular mass of 33.2kDa (Molecular weight on SDS-PAGE will appear higher). The EEF1D is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EEF1D solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Eukaryotic translation elongation factor 1 delta (EEF1D) is a subunit of the elongation factor-1 complex that is responsible for the enzymatic transport of aminoacyl tRNAs to the ribosome. EEF1D functions as guanine nucleotide exchange factor. EEF1D interacts with HIV-1 Tat, and consequently represses the translation of host-cell, but not HIV-1, mRNAs. EEF1D overexpression is linked to oesophageal carcinoma and may negatively influence the outcome of medulloblastomas.
Synonyms
Elongation factor 1-delta, EF-1-delta, Antigen NY-CO-4, EEF1D, EF1D, EF-1D, FP1047, FLJ20897.
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 MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI ARARENIQKS LAGSSGPGAS SGTSGDHGEL VVRIASLEVE NQSLRGVVQE LQQAISKLEA RLNVLEKSSP GHRATAPQTQ HVSPMRQVEP PAKKPATPAE DDEDDDIDLF GSDNEEEDKE AAQLREERLR QYAEKKAKKP ALVAKSSILL DVKPWDDETD MAQLEACVRS IQLDGLVWGA SKLVPVGYGI RKLQIQCVVE DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I.

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

Description:

Nudix Type Motif 3 Human Recombinant

Diphosphoinositol polyphosphate phosphohydrolase 1, DIPP-1, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1, Nucleoside diphosphate-linked moiety X motif 3, Nudix motif 3, NUDT3, DIPP, DIPP1.

Product # :

ENZ-071

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Description

NUDT3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids (1-172 a.a.) and having a molecular mass of 21.6kDa. The NUDT3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NUDT3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
NUDT3 is a 172 amino acid cytoplasmic protein which is a member of the nudix hydrolase family and DIPP subfamily. NUDT3 functions as a negative regulator of the ERK 1/2 pathway and hydrolyzes 5-phosphoribose 1-diphosphate. NUDT3 is a monomer which binds magnesium as a cofactor. In addition, NUDT3 is widely expressed but can be found at highest levels in the liver, pancreas, brain and heart.
Synonyms
Diphosphoinositol polyphosphate phosphohydrolase 1, DIPP-1, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1, Nucleoside diphosphate-linked moiety X motif 3, Nudix motif 3, NUDT3, DIPP, DIPP1.
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 MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG GGMEPEEEPS VAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV TEVLEDWEDS VNIGRKREWF KIEDAIKVLQ YHKPVQASYF ETLRQGYSAN NGTPVVATTY SVSAQSSMSG IR.

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

Description:

2-Oxo-Acid Dehydrogenase Complex E2 Human Recombinant

Product # :

ENZ-084

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Description

BCOADC-E2 is a Full-length cDNA coding for the mature form of the human BCOADC-E2 protein having a molecular mass of 47,321 Dalton(pH 6.5). BCOADC-E2 protein is fused to a hexa-histidine purification tag.

Source

Sf9 insect cells.

Formulation

DLST (0.91mg/ml) is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

Purity

Greater than 75% as determined by SDS-PAGE.

More Info

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-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.
coating concentration
0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.
Applications
Western blot with anti-M2-Antigen autoantibody-positive patient sera or monoclonal
anti-hexa-His-tag antibody.

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

Description:

Borrelia Afzelii Decorin Binding Protein A Recombinant

Product # :

BOR-010

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Description

Recombinant Borrelia Afzelii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19 kDa. Borrelia Afzelii DbpA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Borrelia Afzelii DbpA is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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.
Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma; suitable for LTT (lymphocyte transformation test).
Applications
Western blot with Lyme positive plasma.

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

Description:

Borrelia Burgdorferi p30 Recombinant

Product # :

BOR-028

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Description

Borrelia Burgdorferi p30 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 29kDa. Borrelia p30 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Borrelia p30 is supplied in 20mM HEPES buffer pH-7.5, 400mM NaCl and 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mostly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The Gram-negative bacterium Borreliella spielmanii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. DbpA, also known as p17 or Osp17, is a heterogeneous protein among the human pathogenic B. burgdorferi sensu lato species.
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.
Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative samples.
Applications
Western blot with Lyme positive plasma.

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

Description:

CD2 Human Recombinant, sf9

T-cell surface antigen CD2, T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, Erythrocyte receptor, Rosette receptor, CD2 antigen, CD2, T11, SRBC.

Product # :

PRO-2390

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Shipped with Ice Packs

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Description

CD2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 194 amino acids (25-209a.a.) and having a molecular mass of 22.3kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa).CD2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CD2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CD2 which is also known as E-rosette receptor, T11 and lymphocytefunction antigen-2 (LFA-2) is expressed on T cells, thymocytes, and subset of natural killer cells. Human CD2 functions as the receptor for sheep erythrocytes, human CD58 (LFA-3), and CD15s (Sialyl Lewis X). p56lck, p59fyn, CD3eta and CD3epsilon are tyrosine-phosphorylated after CD2 stimulation. CD2 plays a role in T cell activation, T- or NK-cell-mediated cytolysis, apoptosis in activated peripheral T cells, and regulation of T cell anergy.
Synonyms
T-cell surface antigen CD2, T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, Erythrocyte receptor, Rosette receptor, CD2 antigen, CD2, T11, SRBC.
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
ADPKEITNAL ETWGALGQDI NLDIPSFQMS DDIDDIKWEK TSDKKKIAQF RKEKETFKEK DTYKLFKNGT LKIKHLKTDD QDIYKVSIYD TKGKNVLEKI FDLKIQERVS KPKISWTCIN TTLTCEVMNG TDPELNLYQD GKHLKLSQRV ITHKWTTSLS AKFKCTAGNK VSKESSVEPV
SCPEKGLDHH HHHH.

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

Description:

Jumonji Domain Containing 6 Human Recombinant

Jumonji Domain Containing 6, Phosphatidylserine Receptor, Jumonji Domain-Containing Protein 6, Histone Arginine Demethylase JMJD6, Peptide-Lysine 5-Dioxygenase JMJD6, JmjC Domain-Containing Protein 6, Lysyl-Hydroxylase JMJD6, PTDSR, PSR, Bifunctional Arginine Demethylase And Lysyl-Hydroxylase JMJD6, Protein PTDSR, EC 1.14.11.-, EC 1.14.11, KIAA0585, PTDSR1, Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC:1.14.11.-).

Product # :

PRO-2183

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Shipped with Ice Packs

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Description

JMJD6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414 a.a) and having a molecular mass of 50.0kDa. JMJD6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

JMJD6 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Jumonji Domain Containing 6, also known as JMJD6 performs as a lysyl-hydroxylase which catalyzes 5-hydroxylation on specific lysine residues of target proteins for instance U2AF2/U2AF65 and LUC7L2, as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Additionally to peptidyl-lysine 5-dioxygenase activity, JMJD6 performs as an RNA hydroxylase, as proposed by its ability to bind single strand RNA. Furthermore, it acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) as well as histone H4 at 'Arg-3' (H4R3me), thus taking a part in histone code.
Synonyms
Jumonji Domain Containing 6, Phosphatidylserine Receptor, Jumonji Domain-Containing Protein 6, Histone Arginine Demethylase JMJD6, Peptide-Lysine 5-Dioxygenase JMJD6, JmjC Domain-Containing Protein 6, Lysyl-Hydroxylase JMJD6, PTDSR, PSR, Bifunctional Arginine Demethylase And Lysyl-Hydroxylase JMJD6, Protein PTDSR, EC 1.14.11.-, EC 1.14.11, KIAA0585, PTDSR1, Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC:1.14.11.-).
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 MGSMNHKSKK RIREAKRSAR PELKDSLDWT RHNYYESFSL SPAAVADNVE RADALQLSVE EFVERYERPY KPVVLLNAQE GWSAQEKWTL ERLKRKYRNQ KFKCGEDNDG YSVKMKMKYY IEYMESTRDD SPLYIFDSSY GEHPKRRKLL EDYKVPKFFT DDLFQYAGEK RRPPYRWFVM GPPRSGTGIH IDPLGTSAWN ALVQGHKRWC LFPTSTPREL IKVTRDEGGN QQDEAITWFN VIYPRTQLPT WPPEFKPLEI LQKPGETVFV PGGWWHVVLN LDTTIAITQN FASSTNFPVV WHKTVRGRPK LSRKWYRILK QEHPELAVLA DSVDLQESTG IASDSSSDSS SSSSSSSSDS DSECESGSEG DGTVHRRKKR RTCSMVGNGD TTSQDDCVSK ERSSSRIRDT CGGRAHP.

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

Description:

Cyclophilin-H Human Recombinant, His Tag

Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

Product # :

ENZ-730

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Shipping Method :

Shipped at Room temp

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Description

PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-177) containing 186 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 20.3kDa (calculated).

Source

Escherichia Coli.

Formulation

Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in phosphate buffered saline pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and increase protein folding. PPIH enzyme is a precise factor of the complex that comprises pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. PPIH possess PPIase activity and acts as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.
Synonyms
Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. PPIH is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASAVANSSPVNP VVFFDVSIGG QEVGRMKIEL FADVVPKTAE NFRQFCTGEF RKDGVPIGYK GSTFHRVIKD FMIQGGDFVN GDGTGVASIY RGPFADENFK LRHSAPGLLS MANSGPSTNG CQFFITCSKC DWLDGKHVVF GKIIDGLLVM RKIENVPTGP NNKPKLPVVI SQCGEM.

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

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