16009-13-5

  • Product Name:Hemin
  • Molecular Formula:C34H32ClFeN4O4
  • Purity:99%
  • Molecular Weight:651.952
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Product Details;

CasNo: 16009-13-5

Molecular Formula: C34H32ClFeN4O4

Appearance: Dark purple crystalline powder

Chinese Manufacturer Supply Hemin,Buy 16009-13-5 Cheapest Price

  • Molecular Formula:C34H32ClFeN4O4
  • Molecular Weight:651.952
  • Appearance/Colour:Dark purple crystalline powder 
  • Melting Point:300 °C 
  • PSA:109.18000 
  • LogP:4.29920 

Hemin(Cas 16009-13-5) Usage

Chemical Properties

Dark purple crystalline powder

Description

Hemin is a chemical compound used in various applications, including blood stain identification, biochemical research, and as a complexing agent. Medically, it is employed for the relief of recurrent attacks of acute intermittent porphyria. Derived from processed red blood cells, Hemin contains a Fe2+ ion within its porphyrin ring and serves as an alternative iron source. Its mechanism of action involves inhibiting the production of porphyrins. Panhematin is a specific product associated with Hemin.

Uses

Relief of Acute Intermittent Porphyria (AIP): Administered as an injection for the relief of recurrent attacks of acute intermittent porphyria associated with the menstrual cycle, particularly when carbohydrate therapy is ineffective.
Alternative Iron Source: Serves as an alternative source of iron within the host.

Biochem/physiol Actions

Hemin, the oxidized version of heme, is an iron-containing prosthetic group for a diverse group of proteins. Free heme, which can be released from hemoglobin following hemolysis, is pro-inflammatory and contributes to iron-derived reactive oxygen species. Free hemin levels may be upregulated in various pathological conditions and can contribute to various inflammatory conditions including vascular disorders, renal failure, and immune-mediated disorders.Hemin may be used to study the expression and represson of heme oxygenase 1 (HO-1) as well as the activity of HO-1. Hematin is the "X factor" required to grown Haemophilus influenzae.

Purification Methods

Hemin is purified by recrystallisation from AcOH. Also, hemin (5g) is shaken in pyridine (25mL) till it dissolves, then CHCl3 (40mL) is added, the container is stoppered and shaken for 5minutes (releasing the stopper occasionally). The solution is filtered under slight suction, and the flask and filter are washed with a little CHCl3 (15mL). During this period, AcOH (300mL) is heated to boiling, and saturated aqueous NaCl (5mL) and conc HCl (4mL) are added. The CHCl3 filtrate is poured in a steady stream, with stirring, into the hot AcOH mixture and set aside for 12hours. The crystals are filtered off, washed with 50% aqueous AcOH (50mL), H2O (100mL), EtOH (25mL), Et2O and dried in air. [Fischer Org Synth Coll Vol III 442 1955, Beilstein 26 III/IV 3048.]

InChI:InChI=1/C34H34N4O4.ClH.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);1H;/q;;+3/p-3/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;;/rC34H32ClFeN4O4/c1-7-21-17(3)26-14-31-22(8-2)19(5)29-13-25-18(4)23(9-11-33(41)42)28(38-25)16-32-24(10-12-34(43)44)20(6)30(15-27(21)37-26)40(32)36(35)39(29)31/h7-8,13-16H,1-2,9-12H2,3-6H3,(H,41,42)(H,43,44)/b25-13-,26-14-,27-15-,28-16-,29-13-,30-15-,31-14-,32-16-

16009-13-5 Relevant articles

Impact of metal ions in porphyrin-based applied materials for visible-light photocatalysis: Key information from ultrafast electronic spectroscopy

Kar, Prasenjit,Sardar, Samim,Alarousu, Erkki,Sun, Jingya,Seddigi, Zaki S.,Ahmed, Saleh A.,Danish, Ekram Y.,Mohammed, Omar F.,Pal, Samir Kumar

, p. 10475 - 10483 (2014/08/18)

ProtoporphyrinIX-zinc oxide (PP-ZnO) nan...

Human heme oxygenase cDNA and induction of its mRNA by hemin

Tadashi YOSHIDA, Peter BIRO, Tirza COHEN, Rita M. MÜLLER, Shigeki SHIBAHARA

, European Journal of Biochemistry, Volume171, Issue3 February 1988 Pages 457-461

In contrast to hemin treatment, heat treatment had no apparent effects in either human cell line on the activity of heme oxygenase and its mRNA levels. These results suggest that human heme oxygenase may not be a heat-shock protein.

16009-13-5 Process route

iron(III) chloride

iron(III) chloride

protoporphyrin IX
553-12-8

protoporphyrin IX

iron(III) protoporphyrin IX chloride
13496-05-4,16009-13-5

iron(III) protoporphyrin IX chloride

Conditions
Conditions Yield
In water; dimethyl sulfoxide; for 12h;
 
L-glutamic acid
56-86-0,21675-62-7,23009-64-5,25104-13-6,84960-48-5,25513-46-6

L-glutamic acid

(SP-5-13)-chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato<sup>(4-)</sup>-N<sub>21</sub>,N<sub>22</sub>,N<sub>23</sub>,N<sub>24</sub>)-ferrate<sup>(2-)</sup>, dihydrogen
16009-13-5

(SP-5-13)-chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N21,N22,N23,N24)-ferrate(2-), dihydrogen

Conditions
Conditions Yield
for 24h; radioactivity investigations with duck blood;
 

16009-13-5 Upstream products

  • 56-86-0
    56-86-0

    L-glutamic acid

  • 553-12-8
    553-12-8

    protoporphyrin IX

16009-13-5 Downstream products

  • 927179-10-0
    927179-10-0

    heme b

  • 15489-90-4
    15489-90-4

    ferriprotoporphyrin IX hydroxide

  • 5522-66-7
    5522-66-7

    protoporphyrin IX dimethyl ester

  • 26280-00-2
    26280-00-2

    biliverdin IXγ dimethyl ester

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